|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
517-635 |
1.51e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.98 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 517 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 596
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184
|
90 100 110
....*....|....*....|....*....|....*....
gi 182662416 597 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
4.91e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 533 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 182662416 613 VAELLLERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1024-1338 |
3.21e-20 |
|
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: 95.24 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1024 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 1103
Cdd:COG5238 166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1104 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 1183
Cdd:COG5238 242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1184 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 1260
Cdd:COG5238 289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182662416 1261 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1338
Cdd:COG5238 361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1045-1306 |
1.89e-18 |
|
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: 88.18 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1045 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 1124
Cdd:cd00116 56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1125 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 1201
Cdd:cd00116 135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1202 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 1280
Cdd:cd00116 209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282
|
250 260
....*....|....*....|....*..
gi 182662416 1281 LDLSANpEISCASLEEL-LSTLQKRPQ 1306
Cdd:cd00116 283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
517-653 |
5.16e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.51 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 517 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 592
Cdd:PHA03095 35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 593 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 653
Cdd:PHA03095 115 KVG---RTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
43-355 |
8.45e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 60.01 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 43 YAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMEDYPAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYD 122
Cdd:COG3914 1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 123 HCQsRDALLQAQAAFEKSLAIVDEELEgtlaqgeLNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIFLAEqnhlyeDLF 202
Cdd:COG3914 81 LEL-AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 203 RARYNLGTIHWRAGQHSQAMRCLEGARECAHTMrkrfmeSECCVVIAQVLQDLGDFLAAKRALKKAYRLgsqKPvQRAAI 282
Cdd:COG3914 147 EAYLNLGEALRRLGRLEEAIAALRRALELDPDN------AEALNNLGNALQDLGRLEEAIAAYRRALEL---DP-DNADA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 283 CQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEQLGDLFSKAGDFPrAAEAYQKQLRFAELLDRPGAERAIIH 355
Cdd:COG3914 217 HSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDDD-PAELLALARAWAQLVAAAAAPELPPP 288
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-590 |
5.03e-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: 5.03e-07
10 20
....*....|....*....|....*....
gi 182662416 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-635 |
1.05e-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: 46.54 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 529 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 594
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 182662416 595 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 635
Cdd:cd22192 166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
668-922 |
2.21e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 668 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 747
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 748 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 827
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 828 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 897
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834
|
250 260
....*....|....*....|....*
gi 182662416 898 LASEPPGSPSTPRVSEPSGDSSAAG 922
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
523-627 |
3.09e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 41.99 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 523 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 595
Cdd:TIGR00870 76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125
|
90 100 110
....*....|....*....|....*....|..
gi 182662416 596 CEGITPLHDALNCGHFEVAELLLERGASVTLR 627
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1072-1141 |
7.09e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 36.35 E-value: 7.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 1072 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 1141
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNlltTLSPGAFSGLP----------SLRYLDLSGNRL 61
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
517-635 |
1.51e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.98 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 517 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 596
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184
|
90 100 110
....*....|....*....|....*....|....*....
gi 182662416 597 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
494-635 |
2.46e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.51 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 494 EDDTDGLTPQLEEDEELQGHLGRRKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYG 573
Cdd:COG0666 52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182662416 574 HLEIVRFLLDHGAAVDDpggQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:COG0666 132 NLEIVKLLLEAGADVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-659 |
2.67e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.95 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 523 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPL 602
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 182662416 603 HDALNCGHFEVAELLLERGASVTLRTRKGLSPLETLQQWVKLYRRDLDLETRQKARA 659
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
533-627 |
4.91e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 533 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 612
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 182662416 613 VAELLLERGASVTLR 627
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1024-1338 |
3.21e-20 |
|
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: 95.24 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1024 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 1103
Cdd:COG5238 166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1104 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 1183
Cdd:COG5238 242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1184 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 1260
Cdd:COG5238 289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182662416 1261 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1338
Cdd:COG5238 361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1045-1306 |
1.89e-18 |
|
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: 88.18 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1045 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 1124
Cdd:cd00116 56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1125 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 1201
Cdd:cd00116 135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1202 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 1280
Cdd:cd00116 209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282
|
250 260
....*....|....*....|....*..
gi 182662416 1281 LDLSANpEISCASLEEL-LSTLQKRPQ 1306
Cdd:cd00116 283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1066-1316 |
3.52e-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: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1066 LKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALLDLSSNHLG--PEGLRQLAMGLPGQATLQsleELDLSMNPLGD 1143
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKGCGLQ---ELDLSDNALGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1144 GCGQSLASLLHAcPLLSTLRLQACGFGPSFFLSHQTALGSAfqdAEHLKTLSLSYNALGAPALARTLQSLPAGTLLH-LE 1222
Cdd:cd00116 96 DGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDL---PPALEKLVLGRNRLEGASCEALAKALRANRDLKeLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1223 LSsvaagkgDSDLMEPVFRYLA---KEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLS 1299
Cdd:cd00116 172 LA-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALAS 243
|
250
....*....|....*..
gi 182662416 1300 TLQKRPQGLSFLGLSGC 1316
Cdd:cd00116 244 ALLSPNISLLTLSLSCN 260
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1039-1203 |
1.10e-12 |
|
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: 70.85 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1039 ELQGLGLSFSACSL--------ALDQAQ-------LTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 1103
Cdd:cd00116 119 GLGDRGLRLLAKGLkdlppaleKLVLGRnrlegasCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1104 DLSSNHLGPEGLRQLAMGLPgqaTLQSLEELDLSMNPLGDGCGQSLAS-LLHACPLLSTLRLQACGFGPSFFLSHQTALg 1182
Cdd:cd00116 199 DLNNNGLTDEGASALAETLA---SLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVL- 274
|
170 180
....*....|....*....|.
gi 182662416 1183 safQDAEHLKTLSLSYNALGA 1203
Cdd:cd00116 275 ---AEKESLLELDLRGNKFGE 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
518-586 |
2.01e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 2.01e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 182662416 518 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 586
Cdd:pfam12796 19 NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
523-635 |
2.80e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.13 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 523 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcEGITPL 602
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK---DGLTAL 256
|
90 100 110
....*....|....*....|....*....|...
gi 182662416 603 HDALNCGHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:COG0666 257 LLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1039-1223 |
3.89e-10 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 63.80 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1039 ELQGLGLSFSACS----LALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaelVAALGTMPSLALLDLSSNHLGpeg 1114
Cdd:COG4886 193 QITDLPEPLGNLTnleeLDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLT--- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1115 lrqlamGLPGQATLQSLEELDLSMNPLGDGCGQSLASLLhacPLLSTLRLQACGFGPSFFLSHQTALGSAFQDAEHLKTL 1194
Cdd:COG4886 264 ------DLPPLANLTNLKTLDLSNNQLTDLKLKELELLL---GLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334
|
170 180
....*....|....*....|....*....
gi 182662416 1195 SLSYNALGAPALARTLQSLPAGTLLHLEL 1223
Cdd:COG4886 335 VTLTTLALSLSLLALLTLLLLLNLLSLLL 363
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
517-653 |
5.16e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.51 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 517 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 592
Cdd:PHA03095 35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 593 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 653
Cdd:PHA03095 115 KVG---RTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
519-637 |
1.61e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.90 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 519 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgc 596
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE-- 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 182662416 597 egiTPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLET 637
Cdd:PHA02874 192 ---SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-618 |
1.67e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.67e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 182662416 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNCGHFEVAELLL 618
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
531-582 |
2.03e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 2.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 182662416 531 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 582
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
544-624 |
3.53e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.83 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 544 RVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGAS 623
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
.
gi 182662416 624 V 624
Cdd:PHA03100 251 I 251
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1054-1339 |
7.22e-09 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 59.56 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1054 LDQAQLTPLLRALKLHTALRELRLAGNRlgdkcvaelvaALGTMPSLALLDLSSNHLG--PEGLRQLamglpgqatlQSL 1131
Cdd:COG4886 80 LLLSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1132 EELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsfflshqTALGSAFQDAEHLKTLSLSYNALGApaLARTLQ 1211
Cdd:COG4886 139 KELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQL---------TDLPEELGNLTNLKELDLSNNQITD--LPEPLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1212 SLPAgtllhlelssvaagkgdsdlmepvfrylakegcaLAHLTLSANHLgdkavRDLCRCLSLCPSLISLDLSANPeisc 1291
Cdd:COG4886 203 NLTN----------------------------------LEELDLSGNQL-----TDLPEPLANLTNLETLDLSNNQ---- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 182662416 1292 asLEEL--LSTLQKrpqgLSFLGLSGCAVQG-PLGLGLwdkiaAQLRELQL 1339
Cdd:COG4886 240 --LTDLpeLGNLTN----LEELDLSNNQLTDlPPLANL-----TNLKTLDL 279
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
943-1213 |
7.95e-09 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 59.56 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 943 LFLIPVPHSSDTHSVAWLAEQAAQRYYQTCGLLPRLTLRKEGALLAPQDLIPDVLQSNDEVLAEVTSWDLPPLTDRYRRA 1022
Cdd:COG4886 26 LLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1023 CQSLGQGEHQQVL--QAVELQGLGLSFSAC----SLALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaeLVAALGT 1096
Cdd:COG4886 106 NEELSNLTNLESLdlSGNQLTDLPEELANLtnlkELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1097 MPSLALLDLSSNHLG--PEGLRQlamglpgqatLQSLEELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsff 1174
Cdd:COG4886 181 LTNLKELDLSNNQITdlPEPLGN----------LTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL----- 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 182662416 1175 lshqTALgSAFQDAEHLKTLSLSYNALGAPALARTLQSL 1213
Cdd:COG4886 241 ----TDL-PELGNLTNLEELDLSNNQLTDLPPLANLTNL 274
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
43-355 |
8.45e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 60.01 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 43 YAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMEDYPAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYD 122
Cdd:COG3914 1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 123 HCQsRDALLQAQAAFEKSLAIVDEELEgtlaqgeLNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIFLAEqnhlyeDLF 202
Cdd:COG3914 81 LEL-AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 203 RARYNLGTIHWRAGQHSQAMRCLEGARECAHTMrkrfmeSECCVVIAQVLQDLGDFLAAKRALKKAYRLgsqKPvQRAAI 282
Cdd:COG3914 147 EAYLNLGEALRRLGRLEEAIAALRRALELDPDN------AEALNNLGNALQDLGRLEEAIAAYRRALEL---DP-DNADA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 283 CQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEQLGDLFSKAGDFPrAAEAYQKQLRFAELLDRPGAERAIIH 355
Cdd:COG3914 217 HSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDDD-PAELLALARAWAQLVAAAAAPELPPP 288
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1031-1361 |
1.18e-08 |
|
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: 59.03 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1031 HQQVLQAVELQGLGLSfsacslaldqaQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLAL-------- 1102
Cdd:COG5238 86 PTQLLVVDWEGAEEVS-----------PVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggn 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1103 ---LDLSSNHLGPEGLRQLAMGLPGQatlqSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSfflshqt 1179
Cdd:COG5238 155 avhLLGLAARLGLLAAISMAKALQNN----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1180 algsafqdaehlktlslsynalGAPALARTLQSLPagTLLHLELSSVAAGkgDSDLMEpVFRYLaKEGCALAHLTLSANH 1259
Cdd:COG5238 224 ----------------------GAEILAEALKGNK--SLTTLDLSNNQIG--DEGVIA-LAEAL-KNNTTVETLYLSGNQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1260 LGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLSTLQKRpQGLSFLGLSGCAV--QGPLGLGLWDKIAAQLREL 1337
Cdd:COG5238 276 IGAEGAIALAKALQGNTTLTSLDLSVNR-IGDEGAIALAEGLQGN-KTLHTLNLAYNGIgaQGAIALAKALQENTTLHSL 353
|
330 340
....*....|....*....|....
gi 182662416 1338 QLCSRRLCAEDRDALRQLQPSRPG 1361
Cdd:COG5238 354 DLSDNQIGDEGAIALAKYLEGNTT 377
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
531-628 |
1.20e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 531 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegITPLHDALNCGH 610
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214
|
90
....*....|....*...
gi 182662416 611 FEVAELLLERGASVTLRT 628
Cdd:PHA02875 215 IDIVRLFIKRGADCNIMF 232
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
519-618 |
1.70e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 519 GSKWNR--RNDMGETLLHRACIE-------GQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavd 589
Cdd:PTZ00322 63 TPDHNLttEEVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--- 139
|
90 100
....*....|....*....|....*....
gi 182662416 590 DPGGQGCEGITPLHDALNCGHFEVAELLL 618
Cdd:PTZ00322 140 DPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
527-635 |
3.02e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.89 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 527 DMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCEGITPLHDAL 606
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242
|
90 100 110
....*....|....*....|....*....|.
gi 182662416 607 N-CGHFEVAELLLERGASVTLR-TRKGLSPL 635
Cdd:PHA02878 243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
518-636 |
3.15e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 54.29 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 518 KGSKWNRRNDMGETLLHRACIE--GQLRRVQDLVRQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpgg 593
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN---- 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 594 QGCE-----------------GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 636
Cdd:PHA03100 171 AKNRvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
561-589 |
4.52e-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: 47.25 E-value: 4.52e-07
10 20
....*....|....*....|....*....
gi 182662416 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 |
5.03e-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: 5.03e-07
10 20
....*....|....*....|....*....
gi 182662416 562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
519-642 |
5.22e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 519 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG--- 595
Cdd:PHA02874 147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftp 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182662416 596 -------------------------CEGITPLHDALN--CGhFEVAELLLERGASVTLRTRKGLSPLETLQQWV 642
Cdd:PHA02874 227 lhnaiihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
156-411 |
5.33e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 52.32 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 156 ELNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIflaeqnHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTM 235
Cdd:COG0457 2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKAL------ELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 236 rkrfmeSECCVVIAQVLQDLGDFLAAKRALKKAYRLGSQKP---VQRAAICQNLQHVLAVVRLqqqLEEAEGRDPQGAMV 312
Cdd:COG0457 76 ------AEALNNLGLALQALGRYEEALEDYDKALELDPDDAealYNLGLALLELGRYDEAIEA---YERALELDPDDADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 313 ICEqLGDLFSKAGDFPRAAEAYQKQLRFAELLDRPGAERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNVLEEAKT 392
Cdd:COG0457 147 LYN-LGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLL 225
|
250
....*....|....*....
gi 182662416 393 WLNIALSREEAGDAYELLA 411
Cdd:COG0457 226 ALALLLALRLAALALYQYR 244
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
518-635 |
6.02e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 518 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNY-GHLEIVRFLLDHGAAVDdpGGQGC 596
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN--AKSYI 267
|
90 100 110
....*....|....*....|....*....|....*....
gi 182662416 597 EGITPLHDALNCGhfEVAELLLERGASVTLRTRKGLSPL 635
Cdd:PHA02878 268 LGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
530-635 |
7.99e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.07 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 530 ETLLHRACIEGQLRRVQDLVRQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNC 608
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145
|
90 100
....*....|....*....|....*..
gi 182662416 609 GHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
25-230 |
1.03e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 51.55 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 25 EEAALCHQLGELLAGHGRYAEALEQHWQELQLreradDPlGCAVAHRKIGERLAEMEDYPAALQHQHQYLELAHslrnht 104
Cdd:COG0457 6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALEL-----DP-DDAEALYNLGLAYLRLGRYEEALADYEQALELDP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 105 ELQRAWATIGRTHLDIYDHcqsrdalLQAQAAFEKSLAIVDEELEgtlaqgelnemrtrLYLNLGLTFESLQQTALCNDY 184
Cdd:COG0457 74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 182662416 185 FRKSIFLAeqnhlyEDLFRARYNLGTIHWRAGQHSQAMRCLEGARE 230
Cdd:COG0457 133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEA 172
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
562-589 |
1.73e-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: 45.74 E-value: 1.73e-06
10 20
....*....|....*....|....*....
gi 182662416 562 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 589
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
581-636 |
2.89e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.89e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 182662416 581 LLDHGAAvdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 636
Cdd:pfam13857 1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
526-635 |
6.20e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 50.35 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 526 NDMGETLLHRACIEGQLrrVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDA 605
Cdd:PHA02874 90 NGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC---YPIHIA 164
|
90 100 110
....*....|....*....|....*....|
gi 182662416 606 LNCGHFEVAELLLERGASVTLRTRKGLSPL 635
Cdd:PHA02874 165 IKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
578-636 |
3.98e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 182662416 578 VRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 636
Cdd:PTZ00322 98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
197-416 |
4.57e-05 |
|
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: 47.03 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 197 LYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTMRKRFMEseccvvIAQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG2956 37 LDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE------LAQDYLKAGLLDRAEELLEKLLELDPDDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 277 VQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEqLGDLFSKAGDFPRAAEAYQKQLRFAelldrPGAERAiiHV 356
Cdd:COG2956 111 EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE-LAELYLEQGDYDEAIEALEKALKLD-----PDCARA--LL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 357 SLATTLGDMKDHHGAVRHYEEELRLRSGNVleeaktwlnialsreeagDAYELLAPCFQK 416
Cdd:COG2956 183 LLAELYLEQGDYEEAIAALERALEQDPDYL------------------PALPRLAELYEK 224
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
548-603 |
4.71e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 4.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 182662416 548 LVRQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLH 603
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
529-631 |
5.07e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 529 GETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNC 608
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178
|
90 100
....*....|....*....|...
gi 182662416 609 GHFEVAELLLERGASVTLRTRKG 631
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNG 201
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
518-635 |
5.53e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 518 KGSKWNRRNDMGETLLHRAcieGQLRRVQD----LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 593
Cdd:PHA02876 330 LGADVNAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 182662416 594 Q-GcegiTPLHDALnCGH--FEVAELLLERGASVTLRTRKGLSPL 635
Cdd:PHA02876 407 KiG----TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
247-438 |
7.74e-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: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 247 VIAQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQG-AMVICEQLGDLFSKAG 325
Cdd:COG3914 13 AAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLlLAALLELAALLLQALG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 326 DFPRAAEAYQKQLRFAElldrpgaERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNvleeAKTWLNIALSREEAGD 405
Cdd:COG3914 93 RYEEALALYRRALALNP-------DNAEALFNLGNLLLALGRLEEALAALRRALALNPDF----AEAYLNLGEALRRLGR 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 182662416 406 AYELLApCFQKALscAQQAQRPQLQRQ---VLQHLH 438
Cdd:COG3914 162 LEEAIA-ALRRAL--ELDPDNAEALNNlgnALQDLG 194
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
517-590 |
7.88e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.97 E-value: 7.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182662416 517 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:PHA03100 180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
8-339 |
8.03e-05 |
|
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: 46.26 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 8 RQLSKAKAKAQRAGQRREEAALCH-QLGELLAGHGRYAEALEQHwqeLQLRERADDPlgcAVAHRKIGERLAEMEDYPAA 86
Cdd:COG2956 22 GQPDKAIDLLEEALELDPETVEAHlALGNLYRRRGEYDRAIRIH---QKLLERDPDR---AEALLELAQDYLKAGLLDRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 87 LQHqhqYLELAHSLRNHTELQRAWATIgrthldiydhcqsrdalLQAQAAFEKSLAIVDEELEgtlaqgeLNEMRTRLYL 166
Cdd:COG2956 96 EEL---LEKLLELDPDDAEALRLLAEI-----------------YEQEGDWEKAIEVLERLLK-------LGPENAHAYC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 167 NLGLTFESLQQTALCNDYFRKSIFLAEQNhlyedlFRARYNLGTIHWRAGQHSQAMRCLEgarecahtmrkrfmeseccv 246
Cdd:COG2956 149 ELAELYLEQGDYDEAIEALEKALKLDPDC------ARALLLLAELYLEQGDYEEAIAALE-------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 247 viaQVLQDLGDFLAAKRALKKAYRLGSQKPvqraaicqnlqhvlavvRLQQQLEEAEGRDPQGAMVIceQLGDLFSKAGD 326
Cdd:COG2956 203 ---RALEQDPDYLPALPRLAELYEKLGDPE-----------------EALELLRKALELDPSDDLLL--ALADLLERKEG 260
|
330
....*....|...
gi 182662416 327 FPRAAEAYQKQLR 339
Cdd:COG2956 261 LEAALALLERQLR 273
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-635 |
1.05e-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: 46.54 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 529 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 594
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 182662416 595 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 635
Cdd:cd22192 166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
3-232 |
1.37e-04 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 46.52 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 3 LERELRQLSKAKAKAQRAGQRREEAALCHQLGELLAGHGRYAEALE--QHWQELqlreradDPLgCAVAHRKIGERLAEM 80
Cdd:COG3914 54 AAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALAlyRRALAL-------NPD-NAEALFNLGNLLLAL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 81 EDYPAALQHQHQYLELAHslrnhtELQRAWATIGRTHldiydhcQSRDALLQAQAAFEKSLAIVDEELEgtlaqgelnem 160
Cdd:COG3914 126 GRLEEALAALRRALALNP------DFAEAYLNLGEAL-------RRLGRLEEAIAALRRALELDPDNAE----------- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 161 rtrLYLNLGLTFESLQQTALCNDYFRKSIFLA-EQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECA 232
Cdd:COG3914 182 ---ALNNLGNALQDLGRLEEAIAAYRRALELDpDNADAHSNLLFALRQACDWEVYDRFEELLAALARGPSELS 251
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-638 |
1.41e-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: 46.16 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 525 RNDMGETLLHRACIEGQ-------LRRVQDLVRQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192 47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 182662416 592 --GGQGCE---GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLETL 638
Cdd:cd22192 125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1070-1165 |
1.56e-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: 44.78 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1070 TALRELRLAGNRL--GDK-CVA-ELVAALGtmPSLALLDLSSNHLgpEGLRQLAmglpgqaTLQSLEELDLSMNPLGDgc 1145
Cdd:cd21340 90 TNLEELHIENQRLppGEKlTFDpRSLAALS--NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQISD-- 156
|
90 100
....*....|....*....|
gi 182662416 1146 GQSLASLLHACPLLSTLRLQ 1165
Cdd:cd21340 157 LEELLDLLSSWPSLRELDLT 176
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
530-624 |
2.04e-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: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 530 ETLLHRACIEGQLRRVQDLVRQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCEGITPLHD 604
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95
|
90 100
....*....|....*....|
gi 182662416 605 ALNCGHFEVAELLLERGASV 624
Cdd:cd22192 96 AVVNQNLNLVRELIARGADV 115
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
597-629 |
2.20e-04 |
|
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: 39.58 E-value: 2.20e-04
10 20 30
....*....|....*....|....*....|....
gi 182662416 597 EGITPLHDA-LNCGHFEVAELLLERGASVTLRTR 629
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
597-626 |
5.36e-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: 38.72 E-value: 5.36e-04
10 20 30
....*....|....*....|....*....|
gi 182662416 597 EGITPLHDALNCGHFEVAELLLERGASVTL 626
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1208-1297 |
5.66e-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: 42.85 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 1208 RTLQSLpAGTLLHLELSsvaaGKGDSDLMEpvFRYLakegCALAHLTLSANHLGDkaVRDLCRCLSLCPSLISLDLSANP 1287
Cdd:cd21340 113 RSLAAL-SNSLRVLNIS----GNNIDSLEP--LAPL----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179
|
90 100
....*....|....*....|.
gi 182662416 1288 --------E---ISCASLEEL 1297
Cdd:cd21340 180 vckkpkyrDkiiLASKSLEVL 200
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
5-230 |
9.75e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 42.69 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 5 RELRQLSKAKAKAQRAGQ-RREEAALCHQLGELLAGHGRYAEALEQHWQELQLreradDPlGCAVAHRKIGERLAEMEDY 83
Cdd:COG0457 19 RRLGRYEEAIEDYEKALElDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-----DP-DDAEALNNLGLALQALGRY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 84 PAALQHQHQYLELAHslrnhtELQRAWATIGRTHLDIYDHcqsrdalLQAQAAFEKSLaivdeelegtlaqgELNEMRTR 163
Cdd:COG0457 93 EEALEDYDKALELDP------DDAEALYNLGLALLELGRY-------DEAIEAYERAL--------------ELDPDDAD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 182662416 164 LYLNLGLTFESLQQTALCNDYFRKSIFLAEQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARE 230
Cdd:COG0457 146 ALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLA 212
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
291-419 |
9.93e-04 |
|
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: 40.76 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 291 AVVRLQQQLEeAEGRDPQGAMviceQLGDLFSKAGDFPRAAEAYQKQLRFAelldrpgAERAIIHVSLATTLGDMKDHHG 370
Cdd:COG4235 2 AIARLRQALA-ANPNDAEGWL----LLGRAYLRLGRYDEALAAYEKALRLD-------PDNADALLDLAEALLAAGDTEE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 182662416 371 AVRHYEEELRLRSGNvleeAKTWLNIALSREEAGDaYELLAPCFQKALS 419
Cdd:COG4235 70 AEELLERALALDPDN----PEALYLLGLAAFQQGD-YAEAIAAWQKLLA 113
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
668-922 |
2.21e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 668 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 747
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 748 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 827
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 828 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 897
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834
|
250 260
....*....|....*....|....*
gi 182662416 898 LASEPPGSPSTPRVSEPSGDSSAAG 922
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
|
|
| YfgM |
COG2976 |
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
249-354 |
2.55e-03 |
|
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];
Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 40.61 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 249 AQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAicqNLQhvLAVVRLQQ-QLEEA----EGRDPQG--AMVIcEQLGDLF 321
Cdd:COG2976 97 AKAAVDAGDLDKAAAQLQWVLDNAKDPALKALA---RLR--LARVLLAQkKYDEAlatlDAVKPEAfaALYA-ELRGDIL 170
|
90 100 110
....*....|....*....|....*....|...
gi 182662416 322 SKAGDFPRAAEAYQKQLrfaELLDRPGAERAII 354
Cdd:COG2976 171 LAQGDKAEARAAYQKAL---AALPEDAPLRQLL 200
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
523-627 |
3.09e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 41.99 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 523 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 595
Cdd:TIGR00870 76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125
|
90 100 110
....*....|....*....|....*....|..
gi 182662416 596 CEGITPLHDALNCGHFEVAELLLERGASVTLR 627
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
518-590 |
3.13e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 41.09 E-value: 3.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 518 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
3-459 |
4.49e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.77 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 3 LERELRQLSKAKAKAQRAGQRREEAALCHQLGELLagHGRYAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMED 82
Cdd:COG3899 768 LERALAARALAALAALRHGNPPASARAYANLGLLL--LGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGP 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 83 YPAALQHQHQYLEL-------AHSLRNHTELQRAWATIGRTHLDIYDHCQSRDALLQAQAAFEKSLAIVDEELEGTLAQG 155
Cdd:COG3899 846 LREALELLREALEAgletgdaALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAA 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 156 ELNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIFLAEQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTM 235
Cdd:COG3899 926 AAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAA 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 236 RKRFMESECCVVIAQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICE 315
Cdd:COG3899 1006 AAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAA 1085
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 316 QLGDLFSKAGDFPRAAEAYQKQLRFAELLDRPGAERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNVLEEAKTWLN 395
Cdd:COG3899 1086 AALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLA 1165
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182662416 396 IALSREEAGDAYELLAPCFQKALSCAQQAQRPQLQRQVLQHLHTVQLRLQPQEAPETETRLREL 459
Cdd:COG3899 1166 LAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLA 1229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
548-635 |
4.69e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.19 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 548 LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGH-----FEVAELLLERGA 622
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97
|
90
....*....|...
gi 182662416 623 SVTLRTRKGLSPL 635
Cdd:PHA03100 98 NVNAPDNNGITPL 110
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
666-919 |
4.80e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 666 AAASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPGQAAPAMARPRRSRHGPasSSSSSE 745
Cdd:PHA03307 213 ISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGP--ASSSSS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 746 GEDSAGPARPSQKR-PRCSATAQRVAAWTPGPASNreaatastsraayQAAIRGVGSAQSRLGPGPPRGHSKALAPQAal 824
Cdd:PHA03307 291 PRERSPSPSPSSPGsGPAPSSPRASSSSSSSRESS-------------SSSTSSSSESSRGAAVSPGPSPSRSPSPSR-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 825 ipeeeclagdwlelDMPLTRSRRPRPRGTGdNRRPSSTSGSDSEESRPRARAKQVRLTCMQSCSAPVNAG-PSSLASEPP 903
Cdd:PHA03307 356 --------------PPPPADPSSPRKRPRP-SRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGrPRPSPLDAG 420
|
250
....*....|....*.
gi 182662416 904 GSPSTPRVSEPSGDSS 919
Cdd:PHA03307 421 AASGAFYARYPLLTPS 436
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
3-449 |
5.14e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.38 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 3 LERELRQLSKAKAKAQRAGQRREEAALCHQLGELLAGHGRYAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMED 82
Cdd:COG3899 806 YEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAA 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 83 YPAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYDHCQSRDALLQAQAAfekslaivdEELEGTLAQGELNEMRT 162
Cdd:COG3899 886 LAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAA---------AAAAALAAAAAAAALAA 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 163 RLYLNLGLTFESLQQTALCNDYFRKSIFLAEQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTMRKRFMES 242
Cdd:COG3899 957 ALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAAL 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 243 ECCVVIAQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEQLGDLFS 322
Cdd:COG3899 1037 LAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALAL 1116
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 323 KAGDFPRAAEAYQKQLRFAELLDRPGAERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNVLEEAKTWLNIALSREE 402
Cdd:COG3899 1117 AAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALL 1196
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 182662416 403 AGDAYELLAPCFQKALSCAQQAQRPQLQRQVLQHLHTVQLRLQPQEA 449
Cdd:COG3899 1197 AALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1072-1141 |
7.09e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 36.35 E-value: 7.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182662416 1072 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 1141
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNlltTLSPGAFSGLP----------SLRYLDLSGNRL 61
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
5-168 |
7.96e-03 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 39.60 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 5 RELRQLSKAKAKAQRAGQRR-EEAALCHQLGELLAGHGRYAEALEQHWQELQLreradDPlGCAVAHRKIGERLAEMEDY 83
Cdd:COG0457 87 QALGRYEEALEDYDKALELDpDDAEALYNLGLALLELGRYDEAIEAYERALEL-----DP-DDADALYNLGIALEKLGRY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182662416 84 PAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYDHCQSRDALLQAQAAFEKSLAIVDEELEGTLAQGELNEMRTR 163
Cdd:COG0457 161 EEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALAL 240
|
....*
gi 182662416 164 LYLNL 168
Cdd:COG0457 241 YQYRA 245
|
|
| |
