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Conserved domains on  [gi|187426056|gb|ACD05335|]
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hypothetical protein Amuc_1514 [Akkermansia muciniphila ATCC BAA-835]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M60 pfam13402
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
 369-628 1.31e-92

Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.


:

Pssm-ID: 433178 [Multi-domain]  Cd Length: 268  Bit Score: 287.35  E-value: 1.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  369 GAVPSPLFVMGKTTPEQWAEQLENTKAPWGEIRMPRLIVTMPVEQLKQCPDV--QKTAEFLQKNMALQDWIMGWDTKPD- 445
Cdd:pfam13402   1 GAVRAPYFVYGKTTDEEWEEMLRNYPAPWAELDGGRVILTVPSEFLRQLDRLnpQALWRLWDRVMYSVNEVAGLPRRSDg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  446 RLHHPMRFVVDRQISAGAGHSGYPAMA--TKDWTNSIATGSIIHSGSWGLWHELGHNHQ-SPPFTMEG-QTEVSVNIFSM 521
Cdd:pfam13402  81 RVTRPVRFVFDRQISAGFMHAGYPIMAfpPGSASELVNYDSARKSGCWGPLHELGHNFQqRWGWTWPGhTGEVTNNILSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  522 VCEVMGTGKD--------FESCWGGGMGPYGMSAEMKKYFSGTQTYneapnkvqLFFWVELMYYLGFDAFRQVALQFHDK 593
Cdd:pfam13402 161 YVQELLTGIDstrqinfnGRARWGPALGGWARDKHAKEYLNKGKDL--------LVFYGQLLYYFGWDFYRKLFRAYRTQ 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 187426056  594 PYDNGELSDEKKWEWVMNAFSKVTGKNMGPFFKIW 628
Cdd:pfam13402 233 PYLPRNNSDGDKMSEFMLTFSKVAKRDLRPFFKAW 267
M60-like_N pfam17291
N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.
 261-368 5.72e-34

N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.


:

Pssm-ID: 435844 [Multi-domain]  Cd Length: 106  Bit Score: 125.14  E-value: 5.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  261 NGAQTVRRTVEIDSNIGGWHSTGLYAPPGAEISCSLSGaPKDGSISVRIGCHTDSLHKLDEWKRVPEITMQVPAGRGRVK 340
Cdd:pfam17291   1 NNATREKARVRINSRYSDWQSTGLYAPPGELITIEVPD-NAVGKLVVQIGCHTDNLGHADELFRPPVVTCRFPLDEGVNK 79

                          90       100
                  ....*....|....*....|....*...
gi 187426056  341 MVNPMGGLVYVNVGQRPRRGKvFKVQIS 368
Cdd:pfam17291  80 ISWPYGGLIYIIVPIDTFEGA-VEVTIS 106
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 54-119 9.89e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 51.07  E-value: 9.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056   54 KRKAAQEltaERKLKEKKAREA-AEKQRIKREREiREKKEKERLAAQKAyeEAQEEKARQAAEAARK 119
Cdd:pfam20492  42 ERRQAEE---EAERLEQKRQEAeEEKERLEESAE-MEAEEKEQLEAELA--EAQEEIARLEEEVERK 102
 
Name Accession Description Interval E-value
Peptidase_M60 pfam13402
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
 369-628 1.31e-92

Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.


Pssm-ID: 433178 [Multi-domain]  Cd Length: 268  Bit Score: 287.35  E-value: 1.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  369 GAVPSPLFVMGKTTPEQWAEQLENTKAPWGEIRMPRLIVTMPVEQLKQCPDV--QKTAEFLQKNMALQDWIMGWDTKPD- 445
Cdd:pfam13402   1 GAVRAPYFVYGKTTDEEWEEMLRNYPAPWAELDGGRVILTVPSEFLRQLDRLnpQALWRLWDRVMYSVNEVAGLPRRSDg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  446 RLHHPMRFVVDRQISAGAGHSGYPAMA--TKDWTNSIATGSIIHSGSWGLWHELGHNHQ-SPPFTMEG-QTEVSVNIFSM 521
Cdd:pfam13402  81 RVTRPVRFVFDRQISAGFMHAGYPIMAfpPGSASELVNYDSARKSGCWGPLHELGHNFQqRWGWTWPGhTGEVTNNILSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  522 VCEVMGTGKD--------FESCWGGGMGPYGMSAEMKKYFSGTQTYneapnkvqLFFWVELMYYLGFDAFRQVALQFHDK 593
Cdd:pfam13402 161 YVQELLTGIDstrqinfnGRARWGPALGGWARDKHAKEYLNKGKDL--------LVFYGQLLYYFGWDFYRKLFRAYRTQ 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 187426056  594 PYDNGELSDEKKWEWVMNAFSKVTGKNMGPFFKIW 628
Cdd:pfam13402 233 PYLPRNNSDGDKMSEFMLTFSKVAKRDLRPFFKAW 267
M60-like_N pfam17291
N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.
 261-368 5.72e-34

N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.


Pssm-ID: 435844 [Multi-domain]  Cd Length: 106  Bit Score: 125.14  E-value: 5.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  261 NGAQTVRRTVEIDSNIGGWHSTGLYAPPGAEISCSLSGaPKDGSISVRIGCHTDSLHKLDEWKRVPEITMQVPAGRGRVK 340
Cdd:pfam17291   1 NNATREKARVRINSRYSDWQSTGLYAPPGELITIEVPD-NAVGKLVVQIGCHTDNLGHADELFRPPVVTCRFPLDEGVNK 79

                          90       100
                  ....*....|....*....|....*...
gi 187426056  341 MVNPMGGLVYVNVGQRPRRGKvFKVQIS 368
Cdd:pfam17291  80 ISWPYGGLIYIIVPIDTFEGA-VEVTIS 106
SslE_AcfD_Zn_LP NF037974
SslE/AcfD family lipoprotein zinc metalloprotease; Members of this family are surface ...
 255-518 7.41e-27

SslE/AcfD family lipoprotein zinc metalloprotease; Members of this family are surface lipoprotein zinc metalloproteases, from the family that includes accessory colonization factor AcfD from Vibrio cholerae, SslE (YghJ ) from E. coli (Secreted and Surface-associated Lipoprotein from E. coli), and VPA1376 from Vibrio parahaemolyticus. Each is about 1500 amino acids long, and SslE is a known substrate of a type II secretion system (T2SS). SslE is known to have mucinase activity.


Pssm-ID: 468296 [Multi-domain]  Cd Length: 1389  Bit Score: 117.02  E-value: 7.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  255 FPGVPENGAQTVRRTVEIDSNIGGW-----HSTGLYAPPGAEISCSLSGapkDGSISVRIgchTDSL-----HKLDeWKR 324
Cdd:NF037974  938 YPGETSGSGGGATVTIDTNNNTVAYfagnrQSTGLWAPALQEVTVSGGG---EATITVAL---ADDLtgrekHELS-LKR 1010

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  325 VPEITMQVPAGRGR-VKMVNPMGGLVYVnvgqRPRRGKVFKVQI--SGAVPSPLFVMGkttpeQWAEQLeNTKAPWGEIR 401
Cdd:NF037974 1011 PPRMQKSFVYDGGSsLTFTVPYGGLIYI----QPGNSESVESTFsfSGVVKAPLWKNG-----QWVNPL-NSPAPIAEID 1080

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  402 MPRLIVTMPVEQLKQcPDVQKTAEFLqkNM---ALQDWiMGWD-----------TKPDRLHHPMRFVVDRQISAGAGHSG 467
Cdd:NF037974 1081 SGSFIYTTPKANLNA-SDIAQFAKDL--NRfaeDASDF-YGRDegtsdgkhrrfTYSALPNNRHRFVNDVQISIGAAHSG 1156

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187426056  468 YPAMAT---KDWtNSIATGSIihsGSWGLWHELGHNHQSPPFTMEGQTEVSVNI 518
Cdd:NF037974 1157 YPVMNSsfnADS-TSIPTTPL---NDWLLWHEVGHNLAEAPFNVEGATEVTNNL 1206
ImpA_fam_HExGH NF038322
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ...
 266-636 3.91e-16

ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA from Pseudomonas aeruginosa (PA0572 in strain PAO1), a virulence factor that cleaves CD44 on the surface of human macrophages, inhibiting phagocytosis. Members of this family are distinguished by a strong motif, CGxGCSGNPxD, just a few residues upstream of the familiar metalloprotease motif HExxH (typically HELGH here) and completely lacking in more distant homologs of ImpA.


Pssm-ID: 468474 [Multi-domain]  Cd Length: 879  Bit Score: 82.28  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 266 VRRTVEIDSNiGGWHSTGLYAPPGAEISCSLSGAPkDGSISVRIGCH-TDSLHKLDEW-----KRVPEITMQVPAGrGRV 339
Cdd:NF038322 399 ETKTVTLPSK-SGFTAIGRYALPGQTVTVTRTDNS-GATLAVFINTLrSGSTREFDKNgynrpRFLQSPRIPLAPG-ETV 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 340 KMVNPMGGLVYVNVGQRPRRGKVfKVQISGAVPSPlFVMGKTTPEQWAE---QLENTKAPWGEIRMPRLIVTMPVEQLKQ 416
Cdd:NF038322 476 TFTSPYGGPLQLNFSGATAGLTV-TLRFKGVAKHP-HWRDFTDNAQIAAfvaALAAGDFDWAELKTPGFEVHSRLDKMRK 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 417 -----CPDVQKTAEFLQK---------------NMALQDWI------MGWDT-----KPDRLHHpmrFVVDrQISAGAGH 465
Cdd:NF038322 554 sigrwNGDPADYADAIRTyvfnsnhilagfkgpGISLPAEVqdfctaLGWDCtdtihRAPIVQH---FNAD-QATCGYGC 629

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 466 SGYPamatkdwtnSIATGSIIHSGsWGLWHELGHNHQSPPFTMEGQ--TEVSVNIFSMVceVM-----GTGKDfESCWG- 537
Cdd:NF038322 630 SGNP---------YDAYWGFSPLG-WGDSHELGHNLQQGRLRIYGGrsGECSNNIFPYY--SKwryyaETGND-PSCQRl 696

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 538 -------------GGMGPYGMSAEMKK--YFSGTQTYNEApnkvqlfFWVELMYYL-----------GFDAFRqvALQFH 591
Cdd:NF038322 697 dhkdlfallqasrAQADPEAYRADMYQrlWSDGNNGPRMA-------FYIQLAMLAqklglgdtldnGWHLFT--LLYLH 767

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056 592 DKPYDNGeLSDEKKW-----------------------EWVMNAFSKVTGKNMGPFFKIWRTPVSERA 636
Cdd:NF038322 768 ERLFGKA-AASEADWdankaklgfgsyalaeansisnnDFLLVALSKITGRDMRPYFDMWGLPYSDKA 834
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 54-119 9.89e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 51.07  E-value: 9.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056   54 KRKAAQEltaERKLKEKKAREA-AEKQRIKREREiREKKEKERLAAQKAyeEAQEEKARQAAEAARK 119
Cdd:pfam20492  42 ERRQAEE---EAERLEQKRQEAeEEKERLEESAE-MEAEEKEQLEAELA--EAQEEIARLEEEVERK 102
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 52-119 2.48e-07

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: 53.31  E-value: 2.48e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   52 LAKRKAAQELTAERKLKEKKAREAAEKQRIK-------REREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKaaaeakkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
49-119 9.34e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 9.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQK-AYEEAQ---EEKARQAAEAARK 119
Cdd:COG3064   68 AAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKeKAEEAKrkaEEEAKRKAEEERK 142
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 49-119 2.24e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 2.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 59-120 3.05e-04

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: 39.56  E-value: 3.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  59 QELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYeeaqEEKARQAAEAARKL 120
Cdd:cd22249    9 EEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKRER----EEQLKQDEELAKQL 66
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 48-121 2.34e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056    48 YQDNLAKRkaAQELTAERKLKEKKAREAAEKQRIKREREIREKKEkerlAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:smart00935  30 RQAELEKL--EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQ----EFQRKQQKLQQDLQKRQQEELQKIL 97
growth_prot_Scy NF041483
polarized growth protein Scy;
57-119 4.26e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   57 AAQELTAERKLKEKKAREAAE-----KQRIKRERE-IREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:NF041483  697 AAEALAAAQEEAARRRREAEEtlgsaRAEADQERErAREQSEELLASARKRVEEAQAEAQRLVEEADRR 765
 
Name Accession Description Interval E-value
Peptidase_M60 pfam13402
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
 369-628 1.31e-92

Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.


Pssm-ID: 433178 [Multi-domain]  Cd Length: 268  Bit Score: 287.35  E-value: 1.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  369 GAVPSPLFVMGKTTPEQWAEQLENTKAPWGEIRMPRLIVTMPVEQLKQCPDV--QKTAEFLQKNMALQDWIMGWDTKPD- 445
Cdd:pfam13402   1 GAVRAPYFVYGKTTDEEWEEMLRNYPAPWAELDGGRVILTVPSEFLRQLDRLnpQALWRLWDRVMYSVNEVAGLPRRSDg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  446 RLHHPMRFVVDRQISAGAGHSGYPAMA--TKDWTNSIATGSIIHSGSWGLWHELGHNHQ-SPPFTMEG-QTEVSVNIFSM 521
Cdd:pfam13402  81 RVTRPVRFVFDRQISAGFMHAGYPIMAfpPGSASELVNYDSARKSGCWGPLHELGHNFQqRWGWTWPGhTGEVTNNILSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  522 VCEVMGTGKD--------FESCWGGGMGPYGMSAEMKKYFSGTQTYneapnkvqLFFWVELMYYLGFDAFRQVALQFHDK 593
Cdd:pfam13402 161 YVQELLTGIDstrqinfnGRARWGPALGGWARDKHAKEYLNKGKDL--------LVFYGQLLYYFGWDFYRKLFRAYRTQ 232

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 187426056  594 PYDNGELSDEKKWEWVMNAFSKVTGKNMGPFFKIW 628
Cdd:pfam13402 233 PYLPRNNSDGDKMSEFMLTFSKVAKRDLRPFFKAW 267
M60-like_N pfam17291
N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.
 261-368 5.72e-34

N-terminal domain of M60-like peptidases; This accessory domain has a jelly roll topology.


Pssm-ID: 435844 [Multi-domain]  Cd Length: 106  Bit Score: 125.14  E-value: 5.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  261 NGAQTVRRTVEIDSNIGGWHSTGLYAPPGAEISCSLSGaPKDGSISVRIGCHTDSLHKLDEWKRVPEITMQVPAGRGRVK 340
Cdd:pfam17291   1 NNATREKARVRINSRYSDWQSTGLYAPPGELITIEVPD-NAVGKLVVQIGCHTDNLGHADELFRPPVVTCRFPLDEGVNK 79

                          90       100
                  ....*....|....*....|....*...
gi 187426056  341 MVNPMGGLVYVNVGQRPRRGKvFKVQIS 368
Cdd:pfam17291  80 ISWPYGGLIYIIVPIDTFEGA-VEVTIS 106
SslE_AcfD_Zn_LP NF037974
SslE/AcfD family lipoprotein zinc metalloprotease; Members of this family are surface ...
 255-518 7.41e-27

SslE/AcfD family lipoprotein zinc metalloprotease; Members of this family are surface lipoprotein zinc metalloproteases, from the family that includes accessory colonization factor AcfD from Vibrio cholerae, SslE (YghJ ) from E. coli (Secreted and Surface-associated Lipoprotein from E. coli), and VPA1376 from Vibrio parahaemolyticus. Each is about 1500 amino acids long, and SslE is a known substrate of a type II secretion system (T2SS). SslE is known to have mucinase activity.


Pssm-ID: 468296 [Multi-domain]  Cd Length: 1389  Bit Score: 117.02  E-value: 7.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  255 FPGVPENGAQTVRRTVEIDSNIGGW-----HSTGLYAPPGAEISCSLSGapkDGSISVRIgchTDSL-----HKLDeWKR 324
Cdd:NF037974  938 YPGETSGSGGGATVTIDTNNNTVAYfagnrQSTGLWAPALQEVTVSGGG---EATITVAL---ADDLtgrekHELS-LKR 1010

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  325 VPEITMQVPAGRGR-VKMVNPMGGLVYVnvgqRPRRGKVFKVQI--SGAVPSPLFVMGkttpeQWAEQLeNTKAPWGEIR 401
Cdd:NF037974 1011 PPRMQKSFVYDGGSsLTFTVPYGGLIYI----QPGNSESVESTFsfSGVVKAPLWKNG-----QWVNPL-NSPAPIAEID 1080

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  402 MPRLIVTMPVEQLKQcPDVQKTAEFLqkNM---ALQDWiMGWD-----------TKPDRLHHPMRFVVDRQISAGAGHSG 467
Cdd:NF037974 1081 SGSFIYTTPKANLNA-SDIAQFAKDL--NRfaeDASDF-YGRDegtsdgkhrrfTYSALPNNRHRFVNDVQISIGAAHSG 1156

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187426056  468 YPAMAT---KDWtNSIATGSIihsGSWGLWHELGHNHQSPPFTMEGQTEVSVNI 518
Cdd:NF037974 1157 YPVMNSsfnADS-TSIPTTPL---NDWLLWHEVGHNLAEAPFNVEGATEVTNNL 1206
ImpA_fam_HExGH NF038322
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ...
 266-636 3.91e-16

ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA from Pseudomonas aeruginosa (PA0572 in strain PAO1), a virulence factor that cleaves CD44 on the surface of human macrophages, inhibiting phagocytosis. Members of this family are distinguished by a strong motif, CGxGCSGNPxD, just a few residues upstream of the familiar metalloprotease motif HExxH (typically HELGH here) and completely lacking in more distant homologs of ImpA.


Pssm-ID: 468474 [Multi-domain]  Cd Length: 879  Bit Score: 82.28  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 266 VRRTVEIDSNiGGWHSTGLYAPPGAEISCSLSGAPkDGSISVRIGCH-TDSLHKLDEW-----KRVPEITMQVPAGrGRV 339
Cdd:NF038322 399 ETKTVTLPSK-SGFTAIGRYALPGQTVTVTRTDNS-GATLAVFINTLrSGSTREFDKNgynrpRFLQSPRIPLAPG-ETV 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 340 KMVNPMGGLVYVNVGQRPRRGKVfKVQISGAVPSPlFVMGKTTPEQWAE---QLENTKAPWGEIRMPRLIVTMPVEQLKQ 416
Cdd:NF038322 476 TFTSPYGGPLQLNFSGATAGLTV-TLRFKGVAKHP-HWRDFTDNAQIAAfvaALAAGDFDWAELKTPGFEVHSRLDKMRK 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 417 -----CPDVQKTAEFLQK---------------NMALQDWI------MGWDT-----KPDRLHHpmrFVVDrQISAGAGH 465
Cdd:NF038322 554 sigrwNGDPADYADAIRTyvfnsnhilagfkgpGISLPAEVqdfctaLGWDCtdtihRAPIVQH---FNAD-QATCGYGC 629

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 466 SGYPamatkdwtnSIATGSIIHSGsWGLWHELGHNHQSPPFTMEGQ--TEVSVNIFSMVceVM-----GTGKDfESCWG- 537
Cdd:NF038322 630 SGNP---------YDAYWGFSPLG-WGDSHELGHNLQQGRLRIYGGrsGECSNNIFPYY--SKwryyaETGND-PSCQRl 696

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056 538 -------------GGMGPYGMSAEMKK--YFSGTQTYNEApnkvqlfFWVELMYYL-----------GFDAFRqvALQFH 591
Cdd:NF038322 697 dhkdlfallqasrAQADPEAYRADMYQrlWSDGNNGPRMA-------FYIQLAMLAqklglgdtldnGWHLFT--LLYLH 767

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056 592 DKPYDNGeLSDEKKW-----------------------EWVMNAFSKVTGKNMGPFFKIWRTPVSERA 636
Cdd:NF038322 768 ERLFGKA-AASEADWdankaklgfgsyalaeansisnnDFLLVALSKITGRDMRPYFDMWGLPYSDKA 834
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 54-119 9.89e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 51.07  E-value: 9.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056   54 KRKAAQEltaERKLKEKKAREA-AEKQRIKREREiREKKEKERLAAQKAyeEAQEEKARQAAEAARK 119
Cdd:pfam20492  42 ERRQAEE---EAERLEQKRQEAeEEKERLEESAE-MEAEEKEQLEAELA--EAQEEIARLEEEVERK 102
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 52-119 2.48e-07

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: 53.31  E-value: 2.48e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   52 LAKRKAAQELTAERKLKEKKAREAAEKQRIK-------REREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKaaaeakkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
49-119 9.34e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 9.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQK-AYEEAQ---EEKARQAAEAARK 119
Cdd:COG3064   68 AAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKeKAEEAKrkaEEEAKRKAEEERK 142
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
49-120 1.05e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.58  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  49 QDNLAKRKAaqELTAERKLKEKKAREAAEKQRIKR-EREIREKKEKERLAAQKAYEEAQEEKA-------RQAAEAARKL 120
Cdd:COG3064    2 QEALEEKAA--EAAAQERLEQAEAEKRAAAEAEQKaKEEAEEERLAELEAKRQAEEEAREAKAeaeqraaELAAEAAKKL 79
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
52-121 1.67e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.03  E-value: 1.67e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  52 LAKRKAAQELTAERKlkEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG2268  246 LAKKKAEERREAETA--RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKP 313
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 49-119 2.65e-06

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: 49.84  E-value: 2.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056   49 QDNLAKRKAAQEltaERKLKEKKAREAAEKQriKREREIREKKEKERLAAQKAYEE--AQEEKARQAAEAARK 119
Cdd:TIGR02794  91 QKELEQRAAAEK---AAKQAEQAAKQAEEKQ--KQAEEAKAKQAAEAKAKAEAEAErkAKEEAAKQAEEEAKA 158
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 53-121 4.73e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.15  E-value: 4.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056   53 AKRKAAQELTAERKLKEKKAREAAEKQRI--KREREIREKKEKERLAAqKAYEEAQEEKARQ--AAEAARKLQ 121
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLraQQEKAQDEKAERDELRA-KLYQEEQERKERQkeREEAEKKAR 232
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
48-121 6.96e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.10  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  48 YQDNLAKRKAAqELTAERK-----------LKEKKAREAAEKQRIKREREIREKK--EKER-LAAQKAYEEAQEEKARQA 113
Cdd:COG2268  185 YLDALGRRKIA-EIIRDARiaeaeaereteIAIAQANREAEEAELEQEREIETARiaEAEAeLAKKKAEERREAETARAE 263


                 ....*...
gi 187426056 114 AEAARKLQ 121
Cdd:COG2268  264 AEAAYEIA 271
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 36-121 8.94e-06

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 48.98  E-value: 8.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   36 LLVCGAGAGYYLYQDNLAKRKAAQELTAERKLKEKKAR---------EAAEKQRIKREREIREKKEKERLAAQKAYEEA- 105
Cdd:pfam09731 287 SLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEEldklaeelsARLEEVRAADEAQLRLEFEREREEIRESYEEKl 366

                          90
                  ....*....|....*.
gi 187426056  106 QEEKARQAAEAARKLQ 121
Cdd:pfam09731 367 RTELERQAEAHEEHLK 382
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 53-121 1.03e-05

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: 48.30  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   53 AKRKAAQELTAE-RKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:TIGR02794  76 QAEEAEKQRAAEqARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK 145
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 49-119 1.06e-05

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: 47.92  E-value: 1.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056   49 QDNLAKRKAAQ----ELTAERKLKEKKAREAAEKQriKREREIREKKEKERLAAQ---KAYEEAQEEKARQAAEAARK 119
Cdd:TIGR02794  99 AAEKAAKQAEQaakqAEEKQKQAEEAKAKQAAEAK--AKAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKK 174
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
53-121 1.49e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.11  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056  53 AKRKAAQELTAERKLKEKKAREAAEKQR------IKREREIREKKEKERLAAQKAYEEAQ----EEKARQAAEAARKLQ 121
Cdd:COG3064   31 AEQKAKEEAEEERLAELEAKRQAEEEAReakaeaEQRAAELAAEAAKKLAEAEKAAAEAEkkaaAEKAKAAKEAEAAAA 109
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 53-121 1.61e-05

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: 47.53  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   53 AKRKAAQELTA-ERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYE------EAQEEKARQAAEAARKLQ 121
Cdd:TIGR02794  62 AAKKEQERQKKlEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqkQAEEAKAKQAAEAKAKAE 137
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 52-121 1.80e-05

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 45.80  E-value: 1.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   52 LAKRKAAQEltaERKLKEKKAREAAEkqrikREREIREKKEKERLAAQKAYEEaQEEKARQAAEAARKLQ 121
Cdd:pfam09756   3 LGAKKRAKL---ELKEAKRQQREAEE-----EEREEREKLEEKREEEYKEREE-REEEAEKEKEEEERKQ 63
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
49-121 1.87e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 47.73  E-value: 1.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRI-----KREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG3064   90 EKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAeeakrKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 65-127 3.06e-05

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 45.03  E-value: 3.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   65 RKLKEKKAREAAEKQRIKREREI--REKKEKERLAAQKAYE----EAQEEKARQAAEAARKLQEQAERE 127
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAeeEEREEREKLEEKREEEykerEEREEEAEKEKEEEERKQEEEQER 69
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
49-121 3.47e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 3.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056  49 QDNLAKRKAAQEltAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG2268  232 REIETARIAEAE--AELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAERE 302
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 54-119 4.13e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 4.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   54 KRKAAQEltaerKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:pfam13868 198 DEKAERD-----ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER 258
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
49-121 4.47e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.57  E-value: 4.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056  49 QDNLAKRKAAQELTAERklkEKKAREAAEKQRIKR---EREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG3064   15 QERLEQAEAEKRAAAEA---EQKAKEEAEEERLAEleaKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAA 87
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
54-116 5.27e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.19  E-value: 5.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056  54 KRKAAQELTAERKLKEK-KAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEA 116
Cdd:COG3064    1 AQEALEEKAAEAAAQERlEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEA 64
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 52-116 5.73e-05

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: 45.61  E-value: 5.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   52 LAKRKAAQELTA----ERKLKEKKAREAAEKQRIKREREIrEKKEKERLAAQKayeEAQEEKARQAAEA 116
Cdd:TIGR02794 115 EEKQKQAEEAKAkqaaEAKAKAEAEAERKAKEEAAKQAEE-EAKAKAAAEAKK---KAEEAKKKAEAEA 179
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 49-104 6.84e-05

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: 43.49  E-value: 6.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREReIREKKEKERLAAQKAYEE 104
Cdd:pfam05672  87 EREQREQEEQERLQKQKEEAEAKAREEAERQRQEREK-IMQQEEQERLERKKRIEE 141
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 64-116 1.07e-04

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 41.82  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187426056  64 ERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEA 116
Cdd:COG2811    9 EIKEAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEA 61
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 46-120 1.68e-04

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: 44.10  E-value: 1.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   46 YLYqDNLAKRkaaQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAyEEAQEEKARQAAEAARKL 120
Cdd:pfam07946 243 YLI-DKLAKR---AKLRPEALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKK-KEREEKLAKLSPEEQRKY 312
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
49-120 1.73e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.48  E-value: 1.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKRER-EIREKKEKERLAAQKAYE---EAQEEKARQAAEAARKL 120
Cdd:COG2268  271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEaDVRKPAEAEKQAAEAEAEaeaEAIRAKGLAEAEGKRAL 346
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 54-121 1.77e-04

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: 42.34  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056   54 KRKAAQELtaERKLKEKKAREAAEKQRIKREREiREKKEKERLAAQKAYEEAQEEKARQAA------EAARKLQ 121
Cdd:pfam05672  41 ERLRKEEL--RRRAEEERARREEEARRLEEERR-REEEERQRKAEEEAEEREQREQEEQERlqkqkeEAEAKAR 111
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 58-119 1.82e-04

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: 42.34  E-value: 1.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   58 AQELTAE--RKLKEKKAREaaEKQRIKREREirEKKEKERLAAQKAYEEA-QEEKARQAAEAARK 119
Cdd:pfam05672  12 AARILAEkrRQAREQRERE--EQERLEKEEE--ERLRKEELRRRAEEERArREEEARRLEEERRR 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-125 1.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQEQAE 125
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 49-119 2.24e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 2.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 49-121 2.31e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056   49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 53-121 2.31e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056   53 AKRKAAQeLTAER--KLKEKKAREAAEKqriKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:pfam13868  13 SKLLAAK-CNKERdaQIAEKKRIKAEEK---EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELE 79
rpsP PRK14521
30S ribosomal protein S16; Provisional
 66-117 2.51e-04

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 42.46  E-value: 2.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187426056  66 KLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAA 117
Cdd:PRK14521 118 KDKLSKAKKAAKKAALEAEKKVNEARAEAVAEKKAAEAAAVAAEEAAAAEEE 169
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 49-119 2.55e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  49 QDNLAKRKAAQ-ELTAERKLKEKKAREAAEKQRIK-----REREIREKKEKE---RLAAQKAyEEAQEEKARQAAEAARK 119
Cdd:PRK09510  70 QQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKqlekeRLAAQEQKKQAEeaaKQAALKQ-KQAEEAAAKAAAAAKAK 148
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 59-120 3.05e-04

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: 39.56  E-value: 3.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  59 QELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYeeaqEEKARQAAEAARKL 120
Cdd:cd22249    9 EEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKRER----EEQLKQDEELAKQL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-123 3.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQEQ 123
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PRK12704 PRK12704
phosphodiesterase; Provisional
 33-128 3.76e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  33 LVLLLVCGAGAGYYLYQdNLAKRKAAQ-ELTAERKLKEKK-------------AREAAEKQRIKREREIREKKEK----E 94
Cdd:PRK12704  10 ALVALVVGAVIGYFVRK-KIAEAKIKEaEEEAKRILEEAKkeaeaikkealleAKEEIHKLRNEFEKELRERRNElqklE 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 187426056  95 RLAAQKayEEAQEEKARQAAEAARKLQEQAEREE 128
Cdd:PRK12704  89 KRLLQK--EENLDRKLELLEKREEELEKKEKELE 120
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 53-119 3.91e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 3.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056  53 AKRKAAQEltAERKLKEKKAREAAEKQRIKREREIREKKEKErlAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PRK09510 175 AAKKAAAE--AKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE--AKKKAAAEAKAAAAKAAAEAKAA 237
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 53-119 3.95e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 3.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056  53 AKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PRK09510 167 AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE 233
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
 48-101 4.09e-04

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 40.30  E-value: 4.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   48 YQDNLAKRKAAQELTA-ERKLKEKKarEAAEKQRIKREREIREKK-EKERLAAQKA 101
Cdd:pfam03879  32 WEKRQEKRLELKAIKAkEKELKDEK--EAERQRRIQAIKERREAKeEKERYEELAA 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-124 4.46e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  41 AGAGYYLYQDNLAKRKAAQELTAERK--LKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAAR 118
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365


                 ....*.
gi 187426056 119 KLQEQA 124
Cdd:COG1196  366 ALLEAE 371
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 50-119 4.91e-04

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: 42.91  E-value: 4.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   50 DNLAKRKAAQELTAERKlKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:TIGR02794  44 DPGAVAQQANRIQQQKK-PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK 112
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 32-121 5.47e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.93  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  32 FLVLLLVCGagagYYLY---QDNLAKRKAaqelTAERKLKE-KKAREAAEKQRIKREREIREKKEKerlaAQKAYEEAQE 107
Cdd:COG0711   10 FLILVLLLK----KFAWppiLKALDERQE----KIADGLAEaERAKEEAEAALAEYEEKLAEARAE----AAEIIAEARK 77

                         90
                 ....*....|....
gi 187426056 108 EKARQAAEAARKLQ 121
Cdd:COG0711   78 EAEAIAEEAKAEAE 91
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 52-119 5.53e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.80  E-value: 5.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   52 LAKRKAAQELTAERKLKEkkAREAAEKQRI-----KREREIRE--KKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:pfam15346  28 LEKRKDEIEAEVERRVEE--ARKIMEKQVLeelerEREAELEEerRKEEEERKKREELERILEENNRKIEEAQRK 100
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 53-119 5.84e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 5.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  53 AKRKAAQELTAERKlKEKKAREAAEKQRiKREREIREKKEKErlAAQKAYEEAQ-----EEKARQAAEAARK 119
Cdd:PRK09510 151 AEAKRAAAAAKKAA-AEAKKKAEAEAAK-KAAAEAKKKAEAE--AAAKAAAEAKkkaeaEAKKKAAAEAKKK 218
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 32-116 7.03e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.11  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056  32 FLVLLLVCGagagYYLY---QDNLAKRKAaqelTAERKLKE-KKAREAAEKQRIKREREIREKKEKerlaAQKAYEEAQE 107
Cdd:cd06503    9 FLILLFILK----KFLWkpiLKALDEREE----KIAESLEEaEKAKEEAEELLAEYEEKLAEARAE----AQEIIEEARK 76


                 ....*....
gi 187426056 108 EKARQAAEA 116
Cdd:cd06503   77 EAEKIKEEI 85
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 56-121 8.27e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.79  E-value: 8.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056  56 KAAQELT-AERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQ-------EEKARQAAEAARKLQ 121
Cdd:cd16269  188 QADQALTeKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrqlkekmEEERENLLKEQERAL 261
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 55-119 8.78e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.25  E-value: 8.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056   55 RKAAQELTAERKLKEKKaREAAEKQRIKrEREIR---------EKKEKERLAAQKAYEEAqEEKARQAAEAARK 119
Cdd:pfam15709 429 RRKLQELQRKKQQEEAE-RAEAEKQRQK-ELEMQlaeeqkrlmEMAEEERLEYQRQKQEA-EEKARLEAEERRQ 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-121 1.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056  49 QDNLAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG1196  279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
PTZ00121 PTZ00121
MAEBL; Provisional
 53-118 1.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   53 AKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLaaQKAYEEAQEEKARQAAEAAR 118
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKK 1571
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 54-120 1.16e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  54 KRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQ-----EEKARQAAEAARKL 120
Cdd:PRK09510 116 QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKkkaeaEAAKKAAAEAKKKA 187
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 49-119 1.36e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.53  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056   49 QDNLAK-RKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:pfam05262 240 QDNADKqRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQE 311
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 58-121 1.49e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.18  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   58 AQELTAERKLKEKKAREAAEK----QRIK-REREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:pfam15558 102 DQENQRQEKLERARQEAEQRKqcqeQRLKeKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQ 170
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 65-119 2.03e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056  65 RKLKEKKAREAAEKQRIK----REREIREKK----------EKERLAAQKAYEEAQE------EKARQAAEAARK 119
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKkeqqQAEELQQKQaaeqerlkqlEKERLAAQEQKKQAEEaakqaaLKQKQAEEAAAK 140
PTZ00121 PTZ00121
MAEBL; Provisional
 50-119 2.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056   50 DNLAKRKAAQELTAERKLK---EKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQE----EKARQAAEAARK 119
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKK 1484
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
54-124 2.09e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  54 KRKAAQELTAERKLKEKKAREAAEKQRiKREREIREKKEKERLAAQKAYEEAqEEKARQAAEAARKLQEQA 124
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELR-ERAAELEAEAEEKREAAAEAEEEA-EEAREEVAELNSKLAELK 585
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 54-119 2.10e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  54 KRKAAQEltaERKLKEKKAREAAEKQRIKREREIRE------KKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PRK09510 109 ERLAAQE---QKKQAEEAAKQAALKQKQAEEAAAKAaaaakaKAEAEAKRAAAAAKKAAAEAKKKAEAEAAK 177
HrpB7 pfam09486
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ...
 58-118 2.16e-03

Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.


Pssm-ID: 370523 [Multi-domain]  Cd Length: 157  Bit Score: 39.35  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   58 AQELTAERKLKEKKAREAAEKQRIKR-EREI---REKKEKERLAAQKAYEEAQEEKARQAAEAAR 118
Cdd:pfam09486  93 AALAAARQALDAAEDAVAATRRKIARnDAQLdvcRERIARLRRAAERAREDAADEEAEEAALARR 157
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 48-121 2.34e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056    48 YQDNLAKRkaAQELTAERKLKEKKAREAAEKQRIKREREIREKKEkerlAAQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:smart00935  30 RQAELEKL--EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQ----EFQRKQQKLQQDLQKRQQEELQKIL 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-118 2.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  49 QDNLAKRKAAQELTAERK-LKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAAR 118
Cdd:COG1196  264 ELEAELEELRLELEELELeLEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
rpsP PRK14521
30S ribosomal protein S16; Provisional
 53-117 2.45e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 39.38  E-value: 2.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056  53 AKRKAAQELTAERKLKEKKAREAAEKQ-RIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAA 117
Cdd:PRK14521 112 GKVNAKKDKLSKAKKAAKKAALEAEKKvNEARAEAVAEKKAAEAAAVAAEEAAAAEEEEAEEAPAE 177
PTZ00121 PTZ00121
MAEBL; Provisional
 54-119 2.54e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187426056   54 KRKAAQELTAERKLKEKKAREAAEKQRI---KREREIREKKEKERLAAQKAYEEAQE-----EKARQAAEAARK 119
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKAdeaKKKAEEAKKADEAKKKAEEAKKKADAakkkaEEAKKAAEAAKA 1350
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 50-119 2.92e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 2.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  50 DNLAKRKAAQELTAERKLKE-KKAREAAEKQRIKREREIREKKEKErlaaQKAYEEaQEEKARQAAEAARK 119
Cdd:PRK00409 519 NELIASLEELERELEQKAEEaEALLKEAEKLKEELEEKKEKLQEEE----DKLLEE-AEKEAQQAIKEAKK 584
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-123 2.96e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056  53 AKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQEQ 123
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
32-97 3.05e-03

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 39.55  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056  32 FLVLLLVCGAGAGYYLYQDNLAKRKAA-QELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLA 97
Cdd:COG3167   25 LLLLVLLVLALGYFFLISPQLEELEELeAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELLK 91
PTZ00121 PTZ00121
MAEBL; Provisional
 55-119 3.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056   55 RKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
PTZ00121 PTZ00121
MAEBL; Provisional
 53-119 3.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   53 AKRKAAQELTAER-KLKEKKAREAAE-KQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:PTZ00121 1449 AKKKAEEAKKAEEaKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 9-114 3.42e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.47  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   9 PNPDYMNiPSFSRSVSRGSAVGWFLVLLLVCGAGAGYYLYQDNLakRKAAQELTAERKLKEKKAREAaekqRIKREREIR 88
Cdd:PRK06975 306 PNPPATP-PEPPARRGRGSAALWFVVVVLACAAAVGGYALNRKV--DRLDQELVQRQQANDAQTAEL----RVKTEQAQA 378

                         90       100
                 ....*....|....*....|....*...
gi 187426056  89 EKKEkerLAAQKAYEEAQ--EEKARQAA 114
Cdd:PRK06975 379 SVHQ---LDSQFAQLDGKlaDAQSAQQA 403
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
 82-120 3.81e-03

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 37.90  E-value: 3.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 187426056   82 KREREIREKKEKERLAAQKAYEEAQEEKaRQaaeaARKL 120
Cdd:pfam13892  80 KEERELRKRAEKEALEQAKKEEELREAK-RQ----QRKL 113
PTZ00121 PTZ00121
MAEBL; Provisional
 54-121 4.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056   54 KRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQA----AEAARKLQ 121
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeAEEAKKAE 1705
growth_prot_Scy NF041483
polarized growth protein Scy;
57-119 4.26e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187426056   57 AAQELTAERKLKEKKAREAAE-----KQRIKRERE-IREKKEKERLAAQKAYEEAQEEKARQAAEAARK 119
Cdd:NF041483  697 AAEALAAAQEEAARRRREAEEtlgsaRAEADQERErAREQSEELLASARKRVEEAQAEAQRLVEEADRR 765
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 53-121 4.60e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   53 AKRKAAQELTA-ERKLKEKKAREAAEKQRIKREREIReKKEKERLAAQK-AYEE--------AQEEKARQAAE----AAR 118
Cdd:pfam02841 191 AILQTDQALTAkEKAIEAERAKAEAAEAEQELLREKQ-KEEEQMMEAQErSYQEhvkqliekMEAEREQLLAEqermLEH 269


                  ...
gi 187426056  119 KLQ 121
Cdd:pfam02841 270 KLQ 272
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 52-112 4.71e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 4.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187426056   52 LAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQ 112
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEW 142
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 53-117 5.23e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 5.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187426056  53 AKRKAAQEltAERKLKEKKAREAAEKQRIKREREIREKKEKerlAAQKAYEEAQEEKARQAAEAA 117
Cdd:PRK09510 191 AAAKAAAE--AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAK---AAAEAKAAAEKAAAAKAAEKA 250
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 54-127 5.57e-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: 38.10  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   54 KRKAAQE----LTAERKLKEKKAREAAEKQRIKRE-REIREKKEKERLAAQKAYEEAQEEKARQAAEAAR------KLQE 122
Cdd:pfam05672  49 RRRAEEErarrEEEARRLEEERRREEEERQRKAEEeAEEREQREQEEQERLQKQKEEAEAKAREEAERQRqerekiMQQE 128


                  ....*
gi 187426056  123 QAERE 127
Cdd:pfam05672 129 EQERL 133
MFAP1 pfam06991
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ...
 53-119 5.81e-03

Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.


Pssm-ID: 462060 [Multi-domain]  Cd Length: 215  Bit Score: 38.69  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   53 AKRKAAQELTAERKLKEKKAREAAEKQ---------------------------RIKREREIREKKEKERLAAQK----- 100
Cdd:pfam06991  48 ERKKEADKLVEEEIRREAAAKEAGDEDeneedvddtdgldpeaeyeawklrelkRIKRDREEREAREKEREEIERrrnmt 127

                          90
                  ....*....|....*....
gi 187426056  101 AYEEAQEEKARQAAEAARK 119
Cdd:pfam06991 128 EEERLAEDRENPKKQREKK 146
RNase_Y_N pfam12072
RNase Y N-terminal region;
32-127 6.00e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.33  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   32 FLVLLLVCGAGAGYYLYQ----------DNLAKR---KAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEK----E 94
Cdd:pfam12072   5 LAIIALVVGFVVGYLVRKsiaeakigsaEELAKRiieEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNElqrqE 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 187426056   95 RLAAQKayEEAQEEKARQAAEAARKLQEQAERE 127
Cdd:pfam12072  85 RRLLQK--EETLDRKDESLEKKEESLEKKEKEL 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-131 6.50e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056  54 KRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQEEKARQAAEAARKLQEQAEREEREK 131
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
51-121 6.95e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.65  E-value: 6.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187426056  51 NLAKRKAAQELtaeRKLKEKKAREAAEKQRIKREREIREKKEKERLA-AQKAYEEAQEEKARQAAEAARKLQ 121
Cdd:COG1842   29 DQAIRDMEEDL---VEARQALAQVIANQKRLERQLEELEAEAEKWEEkARLALEKGREDLAREALERKAELE 97
PTZ00121 PTZ00121
MAEBL; Provisional
 53-119 7.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187426056   53 AKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERlaAQKAYEEAQEEKARQAAEAARK 119
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED--AKKAEAVKKAEEAKKDAEEAKK 1244
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 50-121 7.52e-03

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 38.43  E-value: 7.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187426056   50 DNLAKRKAAQELTAERKLKEKKAreaaEKQRIK-REREIREKKEKERLAAQKAyEEAQEEKARQaaeaaRKLQ 121
Cdd:pfam08597  42 EEEEEKEKAAKAAAAKAKKKKKS----KKQKIAeKEAERKAEEEAEEEEELTP-EDEAARKLRL-----RKAE 104
PTZ00121 PTZ00121
MAEBL; Provisional
 53-119 7.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187426056   53 AKRKA-----AQELTAERKLKEKKAREAAEKQRIKREREIREKKEKERLAAQKAYEEAQE----EKARQAAEAARK 119
Cdd:PTZ00121 1383 AKKKAeekkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKK 1458
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 48-120 8.37e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.46  E-value: 8.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056  48 YQDNLAK-RKAAQELTAE-RKLKEK---KAREAAEKQRIKREREIREKKEKERlaaQKAYEEAQEEKARQAAEAARKL 120
Cdd:COG0711   57 YEEKLAEaRAEAAEIIAEaRKEAEAiaeEAKAEAEAEAERIIAQAEAEIEQER---AKALAELRAEVADLAVAIAEKI 131
Metal_resist pfam13801
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ...
 33-118 8.93e-03

Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.


Pssm-ID: 433488 [Multi-domain]  Cd Length: 119  Bit Score: 36.50  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187426056   33 LVLLLVCGAGAGYYLYQDN---------LAKRKAAQELTAERKLKEKKAREAAEKQRIKREREIREKKEK-ERLAAQKAY 102
Cdd:pfam13801   2 LNLFLLGALVGAALRGPGGppgggpgrgGMLLRAALGLPAEQRERLRAALRDHARELRALRRELRAARRElAALLAAPPF 81

                          90
                  ....*....|....*.
gi 187426056  103 EEAQEEKARQAAEAAR 118
Cdd:pfam13801  82 DPAAIEAALAEARQAR 97
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 54-115 9.91e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 9.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187426056   54 KRKAAQELTAERKLKEKKAREAA------EKQRIKREREiREKKEKERLAAQKAYEEAQEEKARQAAE 115
Cdd:pfam13868  54 ERALEEEEEKEEERKEERKRYRQeleeqiEEREQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEE 120
 
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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