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Conserved domains on  [gi|1039749547|ref|XP_017172244|]
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tonsoku-like protein isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-485 7.05e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 7.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 452
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039749547  453 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 873-1177 1.45e-18

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 89.85  E-value: 1.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  873 VLHAMDHQSSSPSFSACSLALCQAQLTPLLR---ALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHL 949
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIGDEGIEElaeALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  950 GQEGLRQLVEgssgqaALQN---LEELDLSMNPLGDGCGQALASLLracpmlstlrlqacgfsssfflshqaalggafQD 1026
Cdd:COG5238    249 GDEGVIALAE------ALKNnttVETLYLSGNQIGAEGAIALAKAL--------------------------------QG 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1027 AVHLKTLSLSYNLLGAP---ALARVLQTlpACTLKRLDLSSvaASKSNSGIIePVIKYLtKEGCALAHLTLSANCLGDKA 1103
Cdd:COG5238    291 NTTLTSLDLSVNRIGDEgaiALAEGLQG--NKTLHTLNLAY--NGIGAQGAI-ALAKAL-QENTTLHSLDLSDNQIGDEG 364

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749547 1104 VRELSRCLPCCPSLTSLDLSANpEVSCASLEELLSALQERSqgLSFLGLSGcsiqGPLNSDLWDKIFVQLQELQ 1177
Cdd:COG5238    365 AIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQTNR--LHTLILDG----NLIGAEAQQRLEQLLERIK 431
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
47-300 6.24e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   47 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 126
Cdd:COG0457      3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  127 NQRvtvcqslkYVLAVIQLQQ-QLEEAEgNDLQGAMAI-------CEQLGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 198
Cdd:COG0457     77 EAL--------NNLGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  199 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQ 278
Cdd:COG0457    141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220

                          250       260
                   ....*....|....*....|..
gi 1039749547  279 LQRQILQHLYTVQLKLQPQEAR 300
Cdd:COG0457    221 ELLLLALALLLALRLAALALYQ 242
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 513-772 7.74e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  513 RLQMASSGQASRSSPALQTIPSNHLFDPETSPPSspcPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRH--RPTS 590
Cdd:PHA03247  2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRlgRAAQ 2675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  591 SSSssedednpSPCRPSQKRLRHTTQQ--GEVKIPDPPKSREtatsSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVP 668
Cdd:PHA03247  2676 ASS--------PPQRPRRRAARPTVGSltSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  669 APKTALIPEEEylagewlevdtplTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSV 748
Cdd:PHA03247  2744 VPAGPATPGGP-------------ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                          250       260
                   ....*....|....*....|....
gi 1039749547  749 prTSGPNKENYAAGQPLLLVQPPP 772
Cdd:PHA03247  2811 --VLAPAAALPPAASPAGPLPPPT 2832
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-485 7.05e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 7.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 452
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039749547  453 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
383-477 1.72e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  383 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 462
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 1039749547  463 VAELLIERGASVTLR 477
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 873-1177 1.45e-18

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 89.85  E-value: 1.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  873 VLHAMDHQSSSPSFSACSLALCQAQLTPLLR---ALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHL 949
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIGDEGIEElaeALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  950 GQEGLRQLVEgssgqaALQN---LEELDLSMNPLGDGCGQALASLLracpmlstlrlqacgfsssfflshqaalggafQD 1026
Cdd:COG5238    249 GDEGVIALAE------ALKNnttVETLYLSGNQIGAEGAIALAKAL--------------------------------QG 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1027 AVHLKTLSLSYNLLGAP---ALARVLQTlpACTLKRLDLSSvaASKSNSGIIePVIKYLtKEGCALAHLTLSANCLGDKA 1103
Cdd:COG5238    291 NTTLTSLDLSVNRIGDEgaiALAEGLQG--NKTLHTLNLAY--NGIGAQGAI-ALAKAL-QENTTLHSLDLSDNQIGDEG 364

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749547 1104 VRELSRCLPCCPSLTSLDLSANpEVSCASLEELLSALQERSqgLSFLGLSGcsiqGPLNSDLWDKIFVQLQELQ 1177
Cdd:COG5238    365 AIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQTNR--LHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 905-1195 1.40e-17

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 85.10  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  905 LKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGqEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGC 984
Cdd:cd00116     19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETG-RIPRGLQSLLQGLTKGCGLQELDLSDNALGPDG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  985 GQALASLLRAcPMLSTLRLQACGFSSSfflsHQAALGGAFQD-AVHLKTLSLSYNLLGAPALARVLQTLPA-CTLKRLDL 1062
Cdd:cd00116     98 CGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLEGASCEALAKALRAnRDLKELNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1063 SsvaasksNSGIIEPVIKYLT---KEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPeVSCASLEELLSA 1139
Cdd:cd00116    173 A-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALASA 244

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039749547 1140 LQERSQGLSFLGLSGCSIQGPLNSDLWDKI--FVQLQELQLCTKDLSTKDRDSVCQRL 1195
Cdd:cd00116    245 LLSPNISLLTLSLSCNDITDDGAKDLAEVLaeKESLLELDLRGNKFGEEGAQLLAESL 302
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 394-517 1.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  394 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 473
Cdd:PHA03100   174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039749547  474 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAATMEKRLQMA 517
Cdd:PHA03100   251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
47-300 6.24e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   47 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 126
Cdd:COG0457      3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  127 NQRvtvcqslkYVLAVIQLQQ-QLEEAEgNDLQGAMAI-------CEQLGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 198
Cdd:COG0457     77 EAL--------NNLGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  199 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQ 278
Cdd:COG0457    141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220

                          250       260
                   ....*....|....*....|..
gi 1039749547  279 LQRQILQHLYTVQLKLQPQEAR 300
Cdd:COG0457    221 ELLLLALALLLALRLAALALYQ 242
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 412-440 4.43e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 47.20  E-value: 4.43e-07
                            10        20
                    ....*....|....*....|....*....
gi 1039749547   412 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 440
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 911-1125 2.70e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  911 LRELRLAGNRLgdacATELLATLGTTPNLVLLDLSSNHLGQEglrqLVEG--SSGqaalqNLEELDLSMNPLGDGCGQAL 988
Cdd:PLN00113   334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTGE----IPEGlcSSG-----NLFKLILFSNSLEGEIPKSL 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  989 AsllrACPMLSTLRLQACGFSSS-----------FFL-----SHQAALGGAFQDAVHLKTLSLSYNLL--GAPALARvlq 1050
Cdd:PLN00113   401 G----ACRSLRRVRLQDNSFSGElpseftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKFfgGLPDSFG--- 473

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749547 1051 tlpACTLKRLDLSsvaaSKSNSGIIEPVIKYLTKegcaLAHLTLSANCLGDKAVRELSRclpcCPSLTSLDLSAN 1125
Cdd:PLN00113   474 ---SKRLENLDLS----RNQFSGAVPRKLGSLSE----LMQLKLSENKLSGEIPDELSS----CKKLVSLDLSHN 533
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 375-488 3.48e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  375 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 441
Cdd:cd22192     47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039749547  442 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 488
Cdd:cd22192    125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
TPR_12 pfam13424
Tetratricopeptide repeat;
166-233 8.10e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 8.10e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749547  166 QLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPD-LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRK 233
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDhPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
PHA03247 PHA03247
large tegument protein UL36; Provisional
 513-772 7.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  513 RLQMASSGQASRSSPALQTIPSNHLFDPETSPPSspcPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRH--RPTS 590
Cdd:PHA03247  2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRlgRAAQ 2675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  591 SSSssedednpSPCRPSQKRLRHTTQQ--GEVKIPDPPKSREtatsSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVP 668
Cdd:PHA03247  2676 ASS--------PPQRPRRRAARPTVGSltSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  669 APKTALIPEEEylagewlevdtplTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSV 748
Cdd:PHA03247  2744 VPAGPATPGGP-------------ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                          250       260
                   ....*....|....*....|....
gi 1039749547  749 prTSGPNKENYAAGQPLLLVQPPP 772
Cdd:PHA03247  2811 --VLAPAAALPPAASPAGPLPPPT 2832
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-485 7.05e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 7.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 452
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039749547  453 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-485 8.28e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 8.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 452
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA---QDNDGNTPL 157

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039749547  453 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-509 7.19e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 7.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPL 452
Cdd:COG0666    147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749547  453 HDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAAT 509
Cdd:COG0666    224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
383-477 1.72e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  383 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 462
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 1039749547  463 VAELLIERGASVTLR 477
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
368-485 7.79e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 7.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  368 KVNKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcD 447
Cdd:COG0666     43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK---D 119

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1039749547  448 GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:COG0666    120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 873-1177 1.45e-18

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 89.85  E-value: 1.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  873 VLHAMDHQSSSPSFSACSLALCQAQLTPLLR---ALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHL 949
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIGDEGIEElaeALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  950 GQEGLRQLVEgssgqaALQN---LEELDLSMNPLGDGCGQALASLLracpmlstlrlqacgfsssfflshqaalggafQD 1026
Cdd:COG5238    249 GDEGVIALAE------ALKNnttVETLYLSGNQIGAEGAIALAKAL--------------------------------QG 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1027 AVHLKTLSLSYNLLGAP---ALARVLQTlpACTLKRLDLSSvaASKSNSGIIePVIKYLtKEGCALAHLTLSANCLGDKA 1103
Cdd:COG5238    291 NTTLTSLDLSVNRIGDEgaiALAEGLQG--NKTLHTLNLAY--NGIGAQGAI-ALAKAL-QENTTLHSLDLSDNQIGDEG 364

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749547 1104 VRELSRCLPCCPSLTSLDLSANpEVSCASLEELLSALQERSqgLSFLGLSGcsiqGPLNSDLWDKIFVQLQELQ 1177
Cdd:COG5238    365 AIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQTNR--LHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 905-1195 1.40e-17

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 85.10  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  905 LKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGqEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGC 984
Cdd:cd00116     19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETG-RIPRGLQSLLQGLTKGCGLQELDLSDNALGPDG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  985 GQALASLLRAcPMLSTLRLQACGFSSSfflsHQAALGGAFQD-AVHLKTLSLSYNLLGAPALARVLQTLPA-CTLKRLDL 1062
Cdd:cd00116     98 CGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLEGASCEALAKALRAnRDLKELNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1063 SsvaasksNSGIIEPVIKYLT---KEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPeVSCASLEELLSA 1139
Cdd:cd00116    173 A-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALASA 244

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039749547 1140 LQERSQGLSFLGLSGCSIQGPLNSDLWDKI--FVQLQELQLCTKDLSTKDRDSVCQRL 1195
Cdd:cd00116    245 LLSPNISLLTLSLSCNDITDDGAKDLAEVLaeKESLLELDLRGNKFGEEGAQLLAESL 302
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 830-1157 1.11e-13

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 74.83  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  830 DPIPDVLQSNDEVLAEVTSWDLPPLKDRYRRAC-----LSLGQGEHQQV---LHAMDHQSSSPSFSACSLALCQAQLTPL 901
Cdd:COG5238     91 VVDWEGAEEVSPVALAETATAVATPPPDLRRIMaktleDSLILYLALPRrinLIQVLKDPLGGNAVHLLGLAARLGLLAA 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  902 LRALK--LHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSSGQAALQNLeelDLSMNP 979
Cdd:COG5238    171 ISMAKalQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL---DLSNNQ 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  980 LGDGCGQALASLLRACPMLSTLRLqacgfsSSFFLSHQ--AALGGAFQDAVHLKTLSLSYNLLGAP---ALARVLQTlpA 1054
Cdd:COG5238    248 IGDEGVIALAEALKNNTTVETLYL------SGNQIGAEgaIALAKALQGNTTLTSLDLSVNRIGDEgaiALAEGLQG--N 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1055 CTLKRLDLSSvaasksnsgiiepvikyltkegcalahltlsaNCLGDKAVRELSRCLPCCPSLTSLDLSANpEVSCASLE 1134
Cdd:COG5238    320 KTLHTLNLAY--------------------------------NGIGAQGAIALAKALQENTTLHSLDLSDN-QIGDEGAI 366

                          330       340
                   ....*....|....*....|...
gi 1039749547 1135 ELLSALQERSQgLSFLGLSGCSI 1157
Cdd:COG5238    367 ALAKYLEGNTT-LRELNLGKNNI 388
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
895-1187 8.02e-12

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.81  E-value: 8.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  895 QAQLTPLLRALKLHTALRELRLAGNRlgdacatellaTLGTTPNLVLLDLSSNHLGQ--EGLRQLvegssgqaalQNLEE 972
Cdd:COG4886     82 LSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTDlpEELANL----------TNLKE 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  973 LDLSMNPLGDgcgqaLASLLRACPMLSTLRLQACGFSSsfflshqaaLGGAFQDAVHLKTLSLSYNLLGapALARVLQTL 1052
Cdd:COG4886    141 LDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD---------LPEELGNLTNLKELDLSNNQIT--DLPEPLGNL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1053 PActLKRLDLssvaaskSNSGI--IEPVIKYLTKegcaLAHLTLSANCLGDkaVRELSRclpcCPSLTSLDLSAN----- 1125
Cdd:COG4886    205 TN--LEELDL-------SGNQLtdLPEPLANLTN----LETLDLSNNQLTD--LPELGN----LTNLEELDLSNNqltdl 265

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749547 1126 -PEVSCASLEEL-LSALQERSQGLSFLGLSGCSIQGPLNSDLWDKIFVQLQELQLCTKDLSTKD 1187
Cdd:COG4886    266 pPLANLTNLKTLdLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLL 329
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-436 2.08e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 2.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 436
Cdd:pfam12796   24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
891-1143 2.15e-11

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 67.65  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  891 LALCQAQLTPLLRALKLHTALRELRLAGNRLgdacaTELLATLGTTPNLVLLDLSSNhlgqeglrQLVEGSSGQAALQNL 970
Cdd:COG4886    118 LDLSGNQLTDLPEELANLTNLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNN--------QLTDLPEELGNLTNL 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  971 EELDLSMNPLGDgcgqaLASLLRACPMLSTLRLQACGFSSsfflshqaaLGGAFQDAVHLKTLSLSYNLLGA-PALARvl 1049
Cdd:COG4886    185 KELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD---------LPEPLANLTNLETLDLSNNQLTDlPELGN-- 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1050 qtLPActLKRLDLSsvaaskSN--SGIiePVIKYLTKegcaLAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPE 1127
Cdd:COG4886    249 --LTN--LEELDLS------NNqlTDL--PPLANLTN----LKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312

                          250
                   ....*....|....*.
gi 1039749547 1128 VSCASLEELLSALQER 1143
Cdd:COG4886    313 LLILLLLLTTLLLLLL 328
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 898-1063 7.23e-11

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 65.07  E-value: 7.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  898 LTPLLRALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSsgqAALQNLEELDLSM 977
Cdd:cd00116    154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETL---ASLKSLEVLNLGD 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  978 NPLGDGCGQALASLLRAcpmlstlrlqacgfsssffLSHQaalggafqdavhLKTLSLSYNLLGAPALARVLQTLPA-CT 1056
Cdd:cd00116    231 NNLTDAGAAALASALLS-------------------PNIS------------LLTLSLSCNDITDDGAKDLAEVLAEkES 279


                   ....*..
gi 1039749547 1057 LKRLDLS 1063
Cdd:cd00116    280 LLELDLR 286
Ank_4 pfam13637
Ankyrin repeats (many copies);
381-432 8.36e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 8.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039749547  381 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 432
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 394-517 1.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  394 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 473
Cdd:PHA03100   174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039749547  474 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAATMEKRLQMA 517
Cdd:PHA03100   251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
 381-503 2.34e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  381 TLLHRACiEGQLRRVQDLVKQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPGGQGcdgITPLHDALN-- 457
Cdd:PHA03095    53 LYLHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVG---RTPLHVYLSgf 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039749547  458 CGHFEVAELLIERGASVTLRTRKGLSPLETLqqwvkLYFRDLDLET 503
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
412-468 3.19e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 3.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749547  412 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNCGHFEVAELLI 468
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
47-300 6.24e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   47 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 126
Cdd:COG0457      3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  127 NQRvtvcqslkYVLAVIQLQQ-QLEEAEgNDLQGAMAI-------CEQLGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 198
Cdd:COG0457     77 EAL--------NNLGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  199 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQ 278
Cdd:COG0457    141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220

                          250       260
                   ....*....|....*....|..
gi 1039749547  279 LQRQILQHLYTVQLKLQPQEAR 300
Cdd:COG0457    221 ELLLLALALLLALRLAALALYQ 242
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 371-487 1.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  371 KWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgcdg 448
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE---- 191

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039749547  449 iTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLET 487
Cdd:PHA02874   192 -SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 47-260 3.31e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 56.28  E-value: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   47 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 126
Cdd:COG2956     71 RDPDRAEALLELAQDYLKAGLLDRAEELLE------KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENA 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  127 NqrvtvcqsLKYVLAVIQLQQ-QLEEAEGNdLQGAMAICEQ-------LGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 198
Cdd:COG2956    145 H--------AYCELAELYLEQgDYDEAIEA-LEKALKLDPDcaralllLAELYLEQGDYEEAIAALERALEQ-------D 208

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039749547  199 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAgdAYELL 260
Cdd:COG2956    209 PDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEA--ALALL 268
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 381-478 3.70e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  381 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgITPLHDALNCGH 460
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214

                           90
                   ....*....|....*...
gi 1039749547  461 FEVAELLIERGASVTLRT 478
Cdd:PHA02875   215 IDIVRLFIKRGADCNIMF 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-486 8.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 8.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIE--GQLRRVQDLVKQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpggqGCD- 447
Cdd:PHA03100   100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN-----AKNr 174

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039749547  448 -----------------GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 486
Cdd:PHA03100   175 vnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 376-467 8.60e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 8.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  376 NDMGETLLHRACIE-------GQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDG 448
Cdd:PTZ00322    72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA---DPTLLDKDG 148

                           90
                   ....*....|....*....
gi 1039749547  449 ITPLHDALNCGHFEVAELL 467
Cdd:PTZ00322   149 KTPLELAEENGFREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 380-485 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  380 ETLLHRACIEGQLRRVQDLVKQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNC 458
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145

                           90       100
                   ....*....|....*....|....*..
gi 1039749547  459 GHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:PHA02875   146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 411-439 2.26e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 48.02  E-value: 2.26e-07
                           10        20
                   ....*....|....*....|....*....
gi 1039749547  411 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 439
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 373-492 3.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG------- 445
Cdd:PHA02874   151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplhna 230

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  446 ---------------------CDGITPLHDALN--CGhFEVAELLIERGASVTLRTRKGLSPLETLQQWV 492
Cdd:PHA02874   231 iihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 412-440 4.43e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 47.20  E-value: 4.43e-07
                            10        20
                    ....*....|....*....|....*....
gi 1039749547   412 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 440
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
15-261 5.35e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.32  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   15 YLNLGLTCESLQQTALCNNYFKKSIflaeqnHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESEC 94
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKAL------ELDPDDAEALYNLGLAYLRLGRYEEALADYE------QALELDPDDAEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   95 CVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP---NQRVTVCQSL-KYVLAVIQLQQQLEEAEGNDlqgamAICEQLGDL 170
Cdd:COG0457     79 LNNLGLALQALGRYEEALEDYDKALELDPDDAealYNLGLALLELgRYDEAIEAYERALELDPDDA-----DALYNLGIA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  171 FSKAGDFPKAAEAYQKQLHLAELLNRPDLELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSR 250
Cdd:COG0457    154 LEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233

                          250
                   ....*....|.
gi 1039749547  251 EEAGDAYELLA 261
Cdd:COG0457    234 RLAALALYQYR 244
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 412-439 6.96e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.51  E-value: 6.96e-07
                           10        20
                   ....*....|....*....|....*....
gi 1039749547  412 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 439
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 377-485 7.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 7.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  377 DMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCDGITPLHDAL 456
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1039749547  457 N-CGHFEVAELLIERGASVTLR-TRKGLSPL 485
Cdd:PHA02878   243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
 392-487 1.73e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  392 LRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGH---LEIVRFLLDHGAAVDDPGGQGCdgiTPLHD-ALNCGHFEVAELL 467
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGF---TPLHLyLYNATTLDVIKLL 103

                           90       100
                   ....*....|....*....|
gi 1039749547  468 IERGASVTLRTRKGLSPLET 487
Cdd:PHA03095   104 IKAGADVNAKDKVGRTPLHV 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 29-286 2.42e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 50.50  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   29 ALCNNYFKKSI-FLAEQNHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGD 107
Cdd:COG2956     18 YLLNGQPDKAIdLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQ------KLLERDPDRAEALLELAQDYLKAGL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  108 FLAAKRALKKAYRLGSQKPN---QRVTVCQSLKYVLAVIQLQQQLEEAEGNDlqgAMAICEqLGDLFSKAGDFPKAAEAY 184
Cdd:COG2956     92 LDRAEELLEKLLELDPDDAEalrLLAEIYEQEGDWEKAIEVLERLLKLGPEN---AHAYCE-LAELYLEQGDYDEAIEAL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  185 QKQLHLAELLNRPDLELAVIHVSLattlgdmKDHRKAVHHYEEELRL---------------RKGNALEEAKTWFNIALS 249
Cdd:COG2956    168 EKALKLDPDCARALLLLAELYLEQ-------GDYEEAIAALERALEQdpdylpalprlaelyEKLGDPEEALELLRKALE 240

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1039749547  250 REEAGDAYELLAPCFQKAfCCAQQAQRFqLQRQILQH 286
Cdd:COG2956    241 LDPSDDLLLALADLLERK-EGLEAALAL-LERQLRRH 275
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 364-485 2.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  364 VGRRKVNKWNRRNDMGETLLHRACIEGQLrrVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 443
Cdd:PHA02874    78 IGAHDIIKLLIDNGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039749547  444 QGCdgiTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 485
Cdd:PHA02874   156 NGC---YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
431-486 5.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039749547  431 LLDHGAAvdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 486
Cdd:pfam13857    1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 428-486 1.69e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749547  428 VRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 486
Cdd:PTZ00322    98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
Ank_5 pfam13857
Ankyrin repeats (many copies);
398-453 1.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749547  398 LVKQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLH 453
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 141-267 2.04e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.38  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  141 AVIQLQQQLEeAEGNDLQGAMaiceQLGDLFSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLGDMKDHRK 220
Cdd:COG4235      2 AIARLRQALA-ANPNDAEGWL----LLGRAYLRLGRYDEALAAYEKALRLDP-------DNADALLDLAEALLAAGDTEE 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039749547  221 AVHHYEEELRLRKGNaleeAKTWFNIALSREEAGDaYELLAPCFQKA 267
Cdd:COG4235     70 AEELLERALALDPDN----PEALYLLGLAAFQQGD-YAEAIAAWQKL 111
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 911-1125 2.70e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  911 LRELRLAGNRLgdacATELLATLGTTPNLVLLDLSSNHLGQEglrqLVEG--SSGqaalqNLEELDLSMNPLGDGCGQAL 988
Cdd:PLN00113   334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTGE----IPEGlcSSG-----NLFKLILFSNSLEGEIPKSL 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  989 AsllrACPMLSTLRLQACGFSSS-----------FFL-----SHQAALGGAFQDAVHLKTLSLSYNLL--GAPALARvlq 1050
Cdd:PLN00113   401 G----ACRSLRRVRLQDNSFSGElpseftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKFfgGLPDSFG--- 473

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749547 1051 tlpACTLKRLDLSsvaaSKSNSGIIEPVIKYLTKegcaLAHLTLSANCLGDKAVRELSRclpcCPSLTSLDLSAN 1125
Cdd:PLN00113   474 ---SKRLENLDLS----RNQFSGAVPRKLGSLSE----LMQLKLSENKLSGEIPDELSS----CKKLVSLDLSHN 533
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 375-488 3.48e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  375 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 441
Cdd:cd22192     47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039749547  442 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 488
Cdd:cd22192    125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 373-485 4.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 4.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  373 NRRNDMGETLLHRAcieGQLRRVQD----LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQ-Gcd 447
Cdd:PHA02876   335 NAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKiG-- 409

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039749547  448 giTPLHDALnCGH--FEVAELLIERGASVTLRTRKGLSPL 485
Cdd:PHA02876   410 --TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 909-1004 4.41e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 45.93  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  909 TALRELRLAGNRLGDACATEL----LATLGTTpnLVLLDLSSNHLgqEGLRQLvegssgqAALQNLEELDLSMNPLGDgc 984
Cdd:cd21340     90 TNLEELHIENQRLPPGEKLTFdprsLAALSNS--LRVLNISGNNI--DSLEPL-------APLRNLEQLDASNNQISD-- 156

                           90       100
                   ....*....|....*....|
gi 1039749547  985 GQALASLLRACPMLSTLRLQ 1004
Cdd:cd21340    157 LEELLDLLSSWPSLRELDLT 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 379-481 4.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  379 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNC 458
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178

                           90       100
                   ....*....|....*....|...
gi 1039749547  459 GHFEVAELLIERGASVTLRTRKG 481
Cdd:PHA02875   179 GDIAICKMLLDSGANIDYFGKNG 201
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 447-479 5.26e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 5.26e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039749547  447 DGITPLHDA-LNCGHFEVAELLIERGASVTLRTR 479
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 144-302 5.44e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.30  E-value: 5.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  144 QLQQQLEEAEGNDLQGAMAICEQLGDLFSKAGDFPKAAEAYQKQLHLAellnrPDLelAVIHVSLATTLGDMKDHRKAVH 223
Cdd:COG3914     61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN-----PDN--AEALFNLGNLLLALGRLEEALA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  224 HYEEELRLRKGNALeeakTWFNIALSREEAGDayellapcFQKAFCCAQQAQRFQLQR-QILQHLYTVQLKL-QPQEARD 301
Cdd:COG3914    134 ALRRALALNPDFAE----AYLNLGEALRRLGR--------LEEAIAALRRALELDPDNaEALNNLGNALQDLgRLEEAIA 201


                   .
gi 1039749547  302 T 302
Cdd:COG3914    202 A 202
TPR_12 pfam13424
Tetratricopeptide repeat;
166-233 8.10e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 8.10e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749547  166 QLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPD-LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRK 233
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDhPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 380-474 1.69e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  380 ETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCDGITPLHD 454
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95

                           90       100
                   ....*....|....*....|
gi 1039749547  455 ALNCGHFEVAELLIERGASV 474
Cdd:cd22192     96 AVVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 447-476 2.15e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.15e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039749547   447 DGITPLHDALNCGHFEVAELLIERGASVTL 476
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 1054-1136 2.66e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547 1054 ACTLKRLDLSsvaasKSNSGIIEPvIKYLTkegcALAHLTLSANCLGDkaVRELSRCLPCCPSLTSLDLSANP------- 1126
Cdd:cd21340    119 SNSLRVLNIS-----GNNIDSLEP-LAPLR----NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPvckkpky 186

                           90
                   ....*....|....
gi 1039749547 1127 -E---VSCASLEEL 1136
Cdd:cd21340    187 rDkiiLASKSLEVL 200
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 379-489 3.07e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  379 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRfLLDHGAAVDDPGGQG---C--------- 446
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGdllCtaakrndlt 636

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749547  447 -----------------DGITPLHDALNCGHFEVAELLIERGASVT-LRTRKGLSPLETLQ 489
Cdd:PLN03192   637 amkellkqglnvdsedhQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRE 697
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-440 3.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 3.33e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039749547  373 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 440
Cdd:PHA03100   186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 379-485 4.78e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  379 GETLLHRACIEGQLRRVQDLVKQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 444
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039749547  445 GCDGITPLH-------DALNCGHFEVAELLIERGASVTL---RTRKGLSPL 485
Cdd:cd22192    166 DSLGNTVLHilvlqpnKTFACQMYDLILSYDKEDDLQPLdlvPNNQGLTPF 216
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 99-231 6.31e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.33  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   99 SQVLQDLGDFLAAKRALKKAYRLGSQKPnqrvtvcqSLKYVLAVIQLQQ-QLEEAEgNDLQGAMAIC-------EQLGDL 170
Cdd:COG4783     11 AQALLLAGDYDEAEALLEKALELDPDNP--------EAFALLGEILLQLgDLDEAI-VLLHEALELDpdepearLNLGLA 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749547  171 FSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLGDMKDHRKAVHHYEEELRL 231
Cdd:COG4783     82 LLKAGDYDEALALLEKALKLDP-------EHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 398-485 6.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  398 LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGH-----FEVAELLIERGA 472
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97

                           90
                   ....*....|...
gi 1039749547  473 SVTLRTRKGLSPL 485
Cdd:PHA03100    98 NVNAPDNNGITPL 110
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 389-503 1.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  389 EGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPLHDALNCGHFEVAELLI 468
Cdd:PHA02876   155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI---IALDDLSVLECAVDSKNIDTIKAII 231

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039749547  469 ERGASVtlrTRKGLSPLETLqqwvklyfRDLDLET 503
Cdd:PHA02876   232 DNRSNI---NKNDLSLLKAI--------RNEDLET 255
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 97-186 1.90e-03

Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];


Pssm-ID: 442215 [Multi-domain]  Cd Length: 207  Bit Score: 40.99  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   97 LVSQVLQDLGDFLAAKRALKKAYRLGSQKPnqrvtvcqsLKYV----LAVIQLQQ--------QLEEAEGNDLQGAMAic 164
Cdd:COG2976     95 LLAKAAVDAGDLDKAAAQLQWVLDNAKDPA---------LKALarlrLARVLLAQkkydealaTLDAVKPEAFAALYA-- 163

                           90       100
                   ....*....|....*....|..
gi 1039749547  165 EQLGDLFSKAGDFPKAAEAYQK 186
Cdd:COG2976    164 ELRGDILLAQGDKAEARAAYQK 185
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 15-121 2.39e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   15 YLNLGLTCESLQQTALCNNYFKKSIFLAEqnhlyeDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESEC 94
Cdd:COG3914    115 LFNLGNLLLALGRLEEALAALRRALALNP------DFAEAYLNLGEALRRLGRLEEAIAALR------RALELDPDNAEA 182

                           90       100
                   ....*....|....*....|....*..
gi 1039749547   95 CVLVSQVLQDLGDFLAAKRALKKAYRL 121
Cdd:COG3914    183 LNNLGNALQDLGRLEEAIAAYRRALEL 209
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 53-191 4.51e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.63  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547   53 RARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKPNqrvtv 132
Cdd:COG4783      5 EALYALAQALLLAGDYDEAEALLE------KALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE----- 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749547  133 cqsLKYVLAVIQLQQ-QLEEAEgNDLQGAMA-------ICEQLGDLFSKAGDFPKAAEAYQKQLHLA 191
Cdd:COG4783     74 ---ARLNLGLALLKAgDYDEAL-ALLEKALKldpehpeAYLRLARAYRALGRPDEAIAALEKALELD 136
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 134-255 6.94e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  134 QSLKYVLAVIQLQQQLEEAEGNDLQGAMAICEQLGDLFSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLG 213
Cdd:COG5010     27 YEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDP-------NNPELYYNLALLYS 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039749547  214 DMKDHRKAVHHYEEELRLRKGNaleeAKTWFNIALSREEAGD 255
Cdd:COG5010    100 RSGDKDEAKEYYEKALALSPDN----PNAYSNLAALLLSLGQ 137
PHA03247 PHA03247
large tegument protein UL36; Provisional
 513-772 7.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  513 RLQMASSGQASRSSPALQTIPSNHLFDPETSPPSspcPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRH--RPTS 590
Cdd:PHA03247  2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRlgRAAQ 2675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  591 SSSssedednpSPCRPSQKRLRHTTQQ--GEVKIPDPPKSREtatsSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVP 668
Cdd:PHA03247  2676 ASS--------PPQRPRRRAARPTVGSltSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749547  669 APKTALIPEEEylagewlevdtplTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSV 748
Cdd:PHA03247  2744 VPAGPATPGGP-------------ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                          250       260
                   ....*....|....*....|....
gi 1039749547  749 prTSGPNKENYAAGQPLLLVQPPP 772
Cdd:PHA03247  2811 --VLAPAAALPPAASPAGPLPPPT 2832
 
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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