|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
4.66e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 187608797 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
4.53e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 187608797 613 VAELLIERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1023-1327 |
5.36e-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: 88.31 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1023 VLHAMDHQSSSPSFSACSLALCQAQLTPLLR---ALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHL 1099
Cdd:COG5238 169 AAISMAKALQNNSVETVYLGCNQIGDEGIEElaeALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1100 GQEGLRQLVEgssgqaALQN---LEELDLSMNPLGDGCGQALASLLracpmlstlrlqacgfsssfflshqaalggafQD 1176
Cdd:COG5238 249 GDEGVIALAE------ALKNnttVETLYLSGNQIGAEGAIALAKAL--------------------------------QG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1177 AVHLKTLSLSYNLLGAP---ALARVLQTlpACTLKRLDLSSvaASKSNSGIIePVIKYLtKEGCALAHLTLSANCLGDKA 1253
Cdd:COG5238 291 NTTLTSLDLSVNRIGDEgaiALAEGLQG--NKTLHTLNLAY--NGIGAQGAI-ALAKAL-QENTTLHSLDLSDNQIGDEG 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187608797 1254 VRELSRCLPCCPSLTSLDLSANpEVSCASLEELLSALQERSqgLSFLGLSGcsiqGPLNSDLWDKIFVQLQELQ 1327
Cdd:COG5238 365 AIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQTNR--LHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1055-1345 |
2.88e-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: 84.33 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1055 LKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGqEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGC 1134
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETG-RIPRGLQSLLQGLTKGCGLQELDLSDNALGPDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1135 GQALASLLRAcPMLSTLRLQACGFSSSfflsHQAALGGAFQD-AVHLKTLSLSYNLLGAPALARVLQTLPA-CTLKRLDL 1212
Cdd:cd00116 98 CGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLEGASCEALAKALRAnRDLKELNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1213 SsvaasksNSGIIEPVIKYLT---KEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPeVSCASLEELLSA 1289
Cdd:cd00116 173 A-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALASA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 187608797 1290 LQERSQGLSFLGLSGCSIQGPLNSDLWDKI--FVQLQELQLCTKDLSTKDRDSVCQRL 1345
Cdd:cd00116 245 LLSPNISLLTLSLSCNDITDDGAKDLAEVLaeKESLLELDLRGNKFGEEGAQLLAESL 302
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
544-667 |
1.19e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.46 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 187608797 624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAATMEKRLQMA 667
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
4.03e-09 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.86 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 277 NQRvtvcqslkYVLAVIQLQQ-QLEEAEgNDLQGAMAI-------CEQLGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 348
Cdd:COG0457 77 EAL--------NNLGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 349 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 187608797 429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457 221 ELLLLALALLLALRLAALALYQ 242
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-590 |
4.97e-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: 4.97e-07
10 20
....*....|....*....|....*....
gi 187608797 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1061-1275 |
2.75e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 48.69 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1061 LRELRLAGNRLgdacATELLATLGTTPNLVLLDLSSNHLGQEglrqLVEG--SSGqaalqNLEELDLSMNPLGDGCGQAL 1138
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTGE----IPEGlcSSG-----NLFKLILFSNSLEGEIPKSL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1139 AsllrACPMLSTLRLQACGFSSS-----------FFL-----SHQAALGGAFQDAVHLKTLSLSYNLL--GAPALARvlq 1200
Cdd:PLN00113 401 G----ACRSLRRVRLQDNSFSGElpseftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKFfgGLPDSFG--- 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187608797 1201 tlpACTLKRLDLSsvaaSKSNSGIIEPVIKYLTKegcaLAHLTLSANCLGDKAVRELSRclpcCPSLTSLDLSAN 1275
Cdd:PLN00113 474 ---SKRLENLDLS----RNQFSGAVPRKLGSLSE----LMQLKLSENKLSGEIPDELSS----CKKLVSLDLSHN 533
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-638 |
3.99e-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: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 187608797 592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
46-271 |
4.21e-05 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 48.07 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 46 ALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDIYDHCQ 125
Cdd:COG3914 4 AALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 126 sRDSLLQAQAAFEKSLAIVDEKLEgmltqreLSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIFLAEqnhlyeDLFRAR 205
Cdd:COG3914 84 -AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFAEAY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187608797 206 YNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG3914 150 LNLGEALRRLGRLEEAIAALR------RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.38e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 40.83 E-value: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187608797 316 QLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPD-LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDhPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
663-922 |
6.42e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 663 RLQMASSGQASRSSPALQTIPSNHLFDPETSPPSspcPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRH--RPTS 740
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRlgRAAQ 2675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 741 SSSssedednpSPCRPSQKRLRHTTQQ--GEVKIPDPPKSREtatsSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVP 818
Cdd:PHA03247 2676 ASS--------PPQRPRRRAARPTVGSltSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 819 APKTALIPEEEylagewlevdtplTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSV 898
Cdd:PHA03247 2744 VPAGPATPGGP-------------ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
250 260
....*....|....*....|....
gi 187608797 899 prTSGPNKENYAAGQPLLLVQPPP 922
Cdd:PHA03247 2811 --VLAPAAALPPAASPAGPLPPPT 2832
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
4.66e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
|
90 100 110
....*....|....*....|....*....|...
gi 187608797 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
5.02e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA---QDNDGNTPL 157
|
90 100 110
....*....|....*....|....*....|...
gi 187608797 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-659 |
3.90e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 104.27 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPL 602
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 187608797 603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAAT 659
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
4.53e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 187608797 613 VAELLIERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
518-635 |
3.21e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.63 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 518 KVNKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcD 597
Cdd:COG0666 43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK---D 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 187608797 598 GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1023-1327 |
5.36e-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: 88.31 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1023 VLHAMDHQSSSPSFSACSLALCQAQLTPLLR---ALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHL 1099
Cdd:COG5238 169 AAISMAKALQNNSVETVYLGCNQIGDEGIEElaeALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1100 GQEGLRQLVEgssgqaALQN---LEELDLSMNPLGDGCGQALASLLracpmlstlrlqacgfsssfflshqaalggafQD 1176
Cdd:COG5238 249 GDEGVIALAE------ALKNnttVETLYLSGNQIGAEGAIALAKAL--------------------------------QG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1177 AVHLKTLSLSYNLLGAP---ALARVLQTlpACTLKRLDLSSvaASKSNSGIIePVIKYLtKEGCALAHLTLSANCLGDKA 1253
Cdd:COG5238 291 NTTLTSLDLSVNRIGDEgaiALAEGLQG--NKTLHTLNLAY--NGIGAQGAI-ALAKAL-QENTTLHSLDLSDNQIGDEG 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187608797 1254 VRELSRCLPCCPSLTSLDLSANpEVSCASLEELLSALQERSqgLSFLGLSGcsiqGPLNSDLWDKIFVQLQELQ 1327
Cdd:COG5238 365 AIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQTNR--LHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1055-1345 |
2.88e-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: 84.33 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1055 LKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGqEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGC 1134
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETG-RIPRGLQSLLQGLTKGCGLQELDLSDNALGPDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1135 GQALASLLRAcPMLSTLRLQACGFSSSfflsHQAALGGAFQD-AVHLKTLSLSYNLLGAPALARVLQTLPA-CTLKRLDL 1212
Cdd:cd00116 98 CGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLEGASCEALAKALRAnRDLKELNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1213 SsvaasksNSGIIEPVIKYLT---KEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPeVSCASLEELLSA 1289
Cdd:cd00116 173 A-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALASA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 187608797 1290 LQERSQGLSFLGLSGCSIQGPLNSDLWDKI--FVQLQELQLCTKDLSTKDRDSVCQRL 1345
Cdd:cd00116 245 LLSPNISLLTLSLSCNDITDDGAKDLAEVLaeKESLLELDLRGNKFGEEGAQLLAESL 302
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
980-1307 |
3.67e-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: 73.29 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 980 DPIPDVLQSNDEVLAEVTSWDLPPLKDRYRRAC-----LSLGQGEHQQV---LHAMDHQSSSPSFSACSLALCQAQLTPL 1051
Cdd:COG5238 91 VVDWEGAEEVSPVALAETATAVATPPPDLRRIMaktleDSLILYLALPRrinLIQVLKDPLGGNAVHLLGLAARLGLLAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1052 LRALK--LHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSSGQAALQNLeelDLSMNP 1129
Cdd:COG5238 171 ISMAKalQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL---DLSNNQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1130 LGDGCGQALASLLRACPMLSTLRLqacgfsSSFFLSHQ--AALGGAFQDAVHLKTLSLSYNLLGAP---ALARVLQTlpA 1204
Cdd:COG5238 248 IGDEGVIALAEALKNNTTVETLYL------SGNQIGAEgaIALAKALQGNTTLTSLDLSVNRIGDEgaiALAEGLQG--N 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1205 CTLKRLDLSSvaasksnsgiiepvikyltkegcalahltlsaNCLGDKAVRELSRCLPCCPSLTSLDLSANpEVSCASLE 1284
Cdd:COG5238 320 KTLHTLNLAY--------------------------------NGIGAQGAIALAKALQENTTLHSLDLSDN-QIGDEGAI 366
|
330 340
....*....|....*....|...
gi 187608797 1285 ELLSALQERSQgLSFLGLSGCSI 1307
Cdd:COG5238 367 ALAKYLEGNTT-LRELNLGKNNI 388
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1045-1337 |
1.22e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 68.42 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1045 QAQLTPLLRALKLHTALRELRLAGNRlgdacatellaTLGTTPNLVLLDLSSNHLGQ--EGLRQLvegssgqaalQNLEE 1122
Cdd:COG4886 82 LSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTDlpEELANL----------TNLKE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1123 LDLSMNPLGDgcgqaLASLLRACPMLSTLRLQACGFSSsfflshqaaLGGAFQDAVHLKTLSLSYNLLGapALARVLQTL 1202
Cdd:COG4886 141 LDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD---------LPEELGNLTNLKELDLSNNQIT--DLPEPLGNL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1203 PActLKRLDLssvaaskSNSGI--IEPVIKYLTKegcaLAHLTLSANCLGDkaVRELSRclpcCPSLTSLDLSAN----- 1275
Cdd:COG4886 205 TN--LEELDL-------SGNQLtdLPEPLANLTN----LETLDLSNNQLTD--LPELGN----LTNLEELDLSNNqltdl 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187608797 1276 -PEVSCASLEEL-LSALQERSQGLSFLGLSGCSIQGPLNSDLWDKIFVQLQELQLCTKDLSTKD 1337
Cdd:COG4886 266 pPLANLTNLKTLdLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLL 329
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1041-1293 |
3.50e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 66.88 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1041 LALCQAQLTPLLRALKLHTALRELRLAGNRLgdacaTELLATLGTTPNLVLLDLSSNhlgqeglrQLVEGSSGQAALQNL 1120
Cdd:COG4886 118 LDLSGNQLTDLPEELANLTNLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNN--------QLTDLPEELGNLTNL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1121 EELDLSMNPLGDgcgqaLASLLRACPMLSTLRLQACGFSSsfflshqaaLGGAFQDAVHLKTLSLSYNLLGA-PALARvl 1199
Cdd:COG4886 185 KELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD---------LPEPLANLTNLETLDLSNNQLTDlPELGN-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1200 qtLPActLKRLDLSsvaaskSN--SGIiePVIKYLTKegcaLAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPE 1277
Cdd:COG4886 249 --LTN--LEELDLS------NNqlTDL--PPLANLTN----LKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312
|
250
....*....|....*.
gi 187608797 1278 VSCASLEELLSALQER 1293
Cdd:COG4886 313 LLILLLLLTTLLLLLL 328
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
523-586 |
4.18e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.51 E-value: 4.18e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 586
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
544-667 |
1.19e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.46 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 187608797 624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAATMEKRLQMA 667
Cdd:PHA03100 251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1048-1213 |
1.23e-10 |
|
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: 64.30 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1048 LTPLLRALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSsgqAALQNLEELDLSM 1127
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETL---ASLKSLEVLNLGD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1128 NPLGDGCGQALASLLRAcpmlstlrlqacgfsssffLSHQaalggafqdavhLKTLSLSYNLLGAPALARVLQTLPA-CT 1206
Cdd:cd00116 231 NNLTDAGAAALASALLS-------------------PNIS------------LLTLSLSCNDITDDGAKDLAEVLAEkES 279
|
....*..
gi 187608797 1207 LKRLDLS 1213
Cdd:cd00116 280 LLELDLR 286
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
531-582 |
1.64e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.67 E-value: 1.64e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 187608797 531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 582
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
531-653 |
2.70e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 531 TLLHRACiEGQLRRVQDLVKQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPGGQGcdgITPLHDALN-- 607
Cdd:PHA03095 53 LYLHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVG---RTPLHVYLSgf 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 187608797 608 CGHFEVAELLIERGASVTLRTRKGLSPLETLqqwvkLYFRDLDLET 653
Cdd:PHA03095 129 NINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-618 |
6.52e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.74 E-value: 6.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 187608797 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNCGHFEVAELLI 618
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
521-637 |
1.79e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.52 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 521 KWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgcdg 598
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE---- 191
|
90 100 110
....*....|....*....|....*....|....*....
gi 187608797 599 iTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLET 637
Cdd:PHA02874 192 -SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
197-450 |
4.03e-09 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.86 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG0457 3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 277 NQRvtvcqslkYVLAVIQLQQ-QLEEAEgNDLQGAMAI-------CEQLGDLFSKAGDFPKAAEAYQKQLHLaellnrpD 348
Cdd:COG0457 77 EAL--------NNLGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 349 LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQ 428
Cdd:COG0457 141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
|
250 260
....*....|....*....|..
gi 187608797 429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457 221 ELLLLALALLLALRLAALALYQ 242
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
531-628 |
4.25e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgITPLHDALNCGH 610
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214
|
90
....*....|....*...
gi 187608797 611 FEVAELLIERGASVTLRT 628
Cdd:PHA02875 215 IDIVRLFIKRGADCNIMF 232
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
523-636 |
9.70e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 56.21 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIE--GQLRRVQDLVKQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpggqGCD- 597
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN-----AKNr 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 187608797 598 -----------------GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PHA03100 175 vnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
526-617 |
1.06e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 526 NDMGETLLHRACIE-------GQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDG 598
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA---DPTLLDKDG 148
|
90
....*....|....*....
gi 187608797 599 ITPLHDALNCGHFEVAELL 617
Cdd:PTZ00322 149 KTPLELAEENGFREVVQLL 167
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
530-635 |
1.33e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 530 ETLLHRACIEGQLRRVQDLVKQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNC 608
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145
|
90 100
....*....|....*....|....*..
gi 187608797 609 GHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
523-642 |
3.55e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.20 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG------- 595
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplhna 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 596 ---------------------CDGITPLHDALN--CGhFEVAELLIERGASVTLRTRKGLSPLETLQQWV 642
Cdd:PHA02874 231 iihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
561-589 |
3.64e-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: 47.64 E-value: 3.64e-07
10 20
....*....|....*....|....*....
gi 187608797 561 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 589
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-590 |
4.97e-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: 4.97e-07
10 20
....*....|....*....|....*....
gi 187608797 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
527-635 |
8.84e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 527 DMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCDGITPLHDAL 606
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242
|
90 100 110
....*....|....*....|....*....|.
gi 187608797 607 N-CGHFEVAELLIERGASVTLR-TRKGLSPL 635
Cdd:PHA02878 243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
562-589 |
1.19e-06 |
|
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: 46.13 E-value: 1.19e-06
10 20
....*....|....*....|....*....
gi 187608797 562 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 589
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
542-637 |
1.99e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.95 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 542 LRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGH---LEIVRFLLDHGAAVDDPGGQGCdgiTPLHD-ALNCGHFEVAELL 617
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGF---TPLHLyLYNATTLDVIKLL 103
|
90 100
....*....|....*....|
gi 187608797 618 IERGASVTLRTRKGLSPLET 637
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHV 123
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
165-411 |
2.54e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 50.39 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 165 YLNLGLTCESLQQTALCNNYFKKSIflaeqnHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESEC 244
Cdd:COG0457 11 YNNLGLAYRRLGRYEEAIEDYEKAL------ELDPDDAEALYNLGLAYLRLGRYEEALADYE------QALELDPDDAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 245 CVLVSQVLQDLGDFLAAKRALKKAYRLGSQKP---NQRVTVCQSL-KYVLAVIQLQQQLEEAEGNDlqgamAICEQLGDL 320
Cdd:COG0457 79 LNNLGLALQALGRYEEALEDYDKALELDPDDAealYNLGLALLELgRYDEAIEAYERALELDPDDA-----DALYNLGIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 321 FSKAGDFPKAAEAYQKQLHLAELLNRPDLELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSR 400
Cdd:COG0457 154 LEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233
|
250
....*....|.
gi 187608797 401 EEAGDAYELLA 411
Cdd:COG0457 234 RLAALALYQYR 244
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
514-635 |
3.34e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 51.12 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 514 VGRRKVNKWNRRNDMGETLLHRACIEGQLrrVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 593
Cdd:PHA02874 78 IGAHDIIKLLIDNGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 187608797 594 QGCdgiTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02874 156 NGC---YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
581-636 |
8.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 8.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 187608797 581 LLDHGAAvdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:pfam13857 1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
578-636 |
2.16e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 2.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 187608797 578 VRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PTZ00322 98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1061-1275 |
2.75e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 48.69 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1061 LRELRLAGNRLgdacATELLATLGTTPNLVLLDLSSNHLGQEglrqLVEG--SSGqaalqNLEELDLSMNPLGDGCGQAL 1138
Cdd:PLN00113 334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTGE----IPEGlcSSG-----NLFKLILFSNSLEGEIPKSL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1139 AsllrACPMLSTLRLQACGFSSS-----------FFL-----SHQAALGGAFQDAVHLKTLSLSYNLL--GAPALARvlq 1200
Cdd:PLN00113 401 G----ACRSLRRVRLQDNSFSGElpseftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKFfgGLPDSFG--- 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187608797 1201 tlpACTLKRLDLSsvaaSKSNSGIIEPVIKYLTKegcaLAHLTLSANCLGDKAVRELSRclpcCPSLTSLDLSAN 1275
Cdd:PLN00113 474 ---SKRLENLDLS----RNQFSGAVPRKLGSLSE----LMQLKLSENKLSGEIPDELSS----CKKLVSLDLSHN 533
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
548-603 |
2.88e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 187608797 548 LVKQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLH 603
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-638 |
3.99e-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: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 187608797 592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
46-271 |
4.21e-05 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 48.07 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 46 ALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDIYDHCQ 125
Cdd:COG3914 4 AALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 126 sRDSLLQAQAAFEKSLAIVDEKLEgmltqreLSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIFLAEqnhlyeDLFRAR 205
Cdd:COG3914 84 -AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFAEAY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187608797 206 YNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG3914 150 LNLGEALRRLGRLEEAIAALR------RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
523-635 |
4.89e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 523 NRRNDMGETLLHRAcieGQLRRVQD----LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQ-Gcd 597
Cdd:PHA02876 335 NAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKiG-- 409
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 187608797 598 giTPLHDALnCGH--FEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02876 410 --TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
291-417 |
5.13e-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: 44.23 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 291 AVIQLQQQLEeAEGNDLQGAMaiceQLGDLFSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLGDMKDHRK 370
Cdd:COG4235 2 AIARLRQALA-ANPNDAEGWL----LLGRAYLRLGRYDEALAAYEKALRLDP-------DNADALLDLAEALLAAGDTEE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 187608797 371 AVHHYEEELRLRKGNaleeAKTWFNIALSREEAGDaYELLAPCFQKA 417
Cdd:COG4235 70 AEELLERALALDPDN----PEALYLLGLAAFQQGD-YAEAIAAWQKL 111
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
529-631 |
5.27e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNC 608
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178
|
90 100
....*....|....*....|...
gi 187608797 609 GHFEVAELLIERGASVTLRTRKG 631
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNG 201
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1059-1154 |
6.98e-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: 45.55 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1059 TALRELRLAGNRLGDACATEL----LATLGTTpnLVLLDLSSNHLgqEGLRQLvegssgqAALQNLEELDLSMNPLGDgc 1134
Cdd:cd21340 90 TNLEELHIENQRLPPGEKLTFdprsLAALSNS--LRVLNISGNNI--DSLEPL-------APLRNLEQLDASNNQISD-- 156
|
90 100
....*....|....*....|
gi 187608797 1135 GQALASLLRACPMLSTLRLQ 1154
Cdd:cd21340 157 LEELLDLLSSWPSLRELDLT 176
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
597-629 |
8.16e-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: 41.12 E-value: 8.16e-05
10 20 30
....*....|....*....|....*....|....
gi 187608797 597 DGITPLHDA-LNCGHFEVAELLIERGASVTLRTR 629
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
294-452 |
8.99e-05 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 46.91 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 294 QLQQQLEEAEGNDLQGAMAICEQLGDLFSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLGDMKDHRKAVH 373
Cdd:COG3914 61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNP-------DNAEALFNLGNLLLALGRLEEALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 374 HYEEELRLRKGNALeeakTWFNIALSREEAGDayellapcFQKAFCCAQQAQRFQLQR-QILQHLYTVQLKL-QPQEARD 451
Cdd:COG3914 134 ALRRALALNPDFAE----AYLNLGEALRRLGR--------LEEAIAALRRALELDPDNaEALNNLGNALQDLgRLEEAIA 201
|
.
gi 187608797 452 T 452
Cdd:COG3914 202 A 202
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-234 |
1.44e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 45.00 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 25 EEAAYCHQLGELLASHGRFKDALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 105 ELQRAWATIGRTHLDIYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTALCNNY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 187608797 185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
530-624 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 530 ETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCDGITPLHD 604
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95
|
90 100
....*....|....*....|
gi 187608797 605 ALNCGHFEVAELLIERGASV 624
Cdd:cd22192 96 AVVNQNLNLVRELIARGADV 115
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
316-383 |
2.38e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 40.83 E-value: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187608797 316 QLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPD-LELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRK 383
Cdd:pfam13424 8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDhPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
597-626 |
2.42e-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: 2.42e-04
10 20 30
....*....|....*....|....*....|
gi 187608797 597 DGITPLHDALNCGHFEVAELLIERGASVTL 626
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
529-639 |
3.51e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 45.24 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRfLLDHGAAVDDPGGQG---C--------- 596
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGdllCtaakrndlt 636
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187608797 597 -----------------DGITPLHDALNCGHFEVAELLIERGASVT-LRTRKGLSPLETLQ 639
Cdd:PLN03192 637 amkellkqglnvdsedhQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRE 697
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
523-590 |
3.81e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 3.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187608797 523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1204-1286 |
4.25e-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: 43.24 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 1204 ACTLKRLDLSsvaasKSNSGIIEPvIKYLTkegcALAHLTLSANCLGDkaVRELSRCLPCCPSLTSLDLSANP------- 1276
Cdd:cd21340 119 SNSLRVLNIS-----GNNIDSLEP-LAPLR----NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPvckkpky 186
|
90
....*....|....
gi 187608797 1277 -E---VSCASLEEL 1286
Cdd:cd21340 187 rDkiiLASKSLEVL 200
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-635 |
5.47e-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: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 529 GETLLHRACIEGQLRRVQDLVKQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 594
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 187608797 595 GCDGITPLH-------DALNCGHFEVAELLIERGASVTL---RTRKGLSPL 635
Cdd:cd22192 166 DSLGNTVLHilvlqpnKTFACQMYDLILSYDKEDDLQPLdlvPNNQGLTPF 216
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
548-635 |
7.93e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 548 LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGH-----FEVAELLIERGA 622
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97
|
90
....*....|...
gi 187608797 623 SVTLRTRKGLSPL 635
Cdd:PHA03100 98 NVNAPDNNGITPL 110
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
539-653 |
2.03e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.36 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 539 EGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPLHDALNCGHFEVAELLI 618
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI---IALDDLSVLECAVDSKNIDTIKAII 231
|
90 100 110
....*....|....*....|....*....|....*
gi 187608797 619 ERGASVtlrTRKGLSPLETLqqwvklyfRDLDLET 653
Cdd:PHA02876 232 DNRSNI---NKNDLSLLKAI--------RNEDLET 255
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
249-381 |
2.38e-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: 39.79 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 249 SQVLQDLGDFLAAKRALKKAYRLGSQKPnqrvtvcqSLKYVLAVIQLQQ-QLEEAEgNDLQGAMAIC-------EQLGDL 320
Cdd:COG4783 11 AQALLLAGDYDEAEALLEKALELDPDNP--------EAFALLGEILLQLgDLDEAI-VLLHEALELDpdepearLNLGLA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187608797 321 FSKAGDFPKAAEAYQKQLHLAEllnrpdlELAVIHVSLATTLGDMKDHRKAVHHYEEELRL 381
Cdd:COG4783 82 LLKAGDYDEALALLEKALKLDP-------EHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
32-339 |
2.51e-03 |
|
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: 41.25 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 32 QLGELLASHGRFKDALEEHQQelhLLESVQDTlgcAVAHRKIGERLAEMENYSAALKhqhLYLDLAGSLSNHTELQRAWA 111
Cdd:COG2956 47 ALGNLYRRRGEYDRAIRIHQK---LLERDPDR---AEALLELAQDYLKAGLLDRAEE---LLEKLLELDPDDAEALRLLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 112 TIgrthldiydhcqsrdslLQAQAAFEKSLAIVdEKLEgmltqrELSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIFL 191
Cdd:COG2956 118 EI-----------------YEQEGDWEKAIEVL-ERLL------KLGPENAHAYCELAELYLEQGDYDEAIEALEKALKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 192 AEQNhlyedlFRARYNLGAIHWRGGQHSQAMRCLEgarecaramkmrfmeseccvlvsQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG2956 174 DPDC------ARALLLLAELYLEQGDYEEAIAALE-----------------------RALEQDPDYLPALPRLAELYEK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187608797 272 GSQKPNqrvtvcqslkyvlAVIQLQQQLEEAEGNDLQGAmaiceqLGDLFSKAGDFPKAAEAYQKQLH 339
Cdd:COG2956 225 LGDPEE-------------ALELLRKALELDPSDDLLLA------LADLLERKEGLEAALALLERQLR 273
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
156-382 |
3.48e-03 |
|
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: 40.87 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 156 ELSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIflaeqnHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAM 235
Cdd:COG2956 70 ERDPDRAEALLELAQDYLKAGLLDRAEELLEKLL------ELDPDDAEALRLLAEIYEQEGDWEKAIEVLE------RLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 236 KMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLgsqKPNqrvtvCQSLKYVLAVIQLQQQ--------LEEAEGNDL 307
Cdd:COG2956 138 KLGPENAHAYCELAELYLEQGDYDEAIEALEKALKL---DPD-----CARALLLLAELYLEQGdyeeaiaaLERALEQDP 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187608797 308 QGAMAIcEQLGDLFSKAGDFPKAAEAYQKQLHLAellnrPDLELaviHVSLATTLGDMKDHRKAVHHYEEELRLR 382
Cdd:COG2956 210 DYLPAL-PRLAELYEKLGDPEEALELLRKALELD-----PSDDL---LLALADLLERKEGLEAALALLERQLRRH 275
|
|
| YfgM |
COG2976 |
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
247-336 |
3.99e-03 |
|
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];
Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 40.22 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 247 LVSQVLQDLGDFLAAKRALKKAYRLGSQKPnqrvtvcqsLKYV----LAVIQLQQ--------QLEEAEGNDLQGAMAic 314
Cdd:COG2976 95 LLAKAAVDAGDLDKAAAQLQWVLDNAKDPA---------LKALarlrLARVLLAQkkydealaTLDAVKPEAFAALYA-- 163
|
90 100
....*....|....*....|..
gi 187608797 315 EQLGDLFSKAGDFPKAAEAYQK 336
Cdd:COG2976 164 ELRGDILLAQGDKAEARAAYQK 185
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
663-922 |
6.42e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 663 RLQMASSGQASRSSPALQTIPSNHLFDPETSPPSspcPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRH--RPTS 740
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRlgRAAQ 2675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 741 SSSssedednpSPCRPSQKRLRHTTQQ--GEVKIPDPPKSREtatsSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVP 818
Cdd:PHA03247 2676 ASS--------PPQRPRRRAARPTVGSltSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608797 819 APKTALIPEEEylagewlevdtplTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSV 898
Cdd:PHA03247 2744 VPAGPATPGGP-------------ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
250 260
....*....|....*....|....
gi 187608797 899 prTSGPNKENYAAGQPLLLVQPPP 922
Cdd:PHA03247 2811 --VLAPAAALPPAASPAGPLPPPT 2832
|
|
|