NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568936357|ref|XP_006535353|]
View 

ankyrin repeat domain-containing protein 17 isoform X5 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-553 7.26e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 7.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568936357  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 1.53e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568936357  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1277 1.92e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  989 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1068
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1069 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1148
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1149 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1228
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1229 KGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPL 1277
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1613-1683 9.21e-40

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


:

Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 142.20  E-value: 9.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1683
Cdd:cd22502     1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 5.01e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 568936357   601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1953-2335 4.58e-12

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 72.28  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1953 ASPNKGASASEQEASSPPVVePANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRP------------PLQQSQVPSPDV 2020
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAA-PDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPrapvddrgdprgPAPPSPLPPDTH 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2021 RMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPA-IRPPSHAT--AAPHKTPAPvQSSSASVLNVNHIKRP 2097
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrARRLGRAAqaSSPPQRPRR-RAARPTVGSLTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2098 HS---------VPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSA--------------PLPFGPFStlfennPTNAHAF 2154
Cdd:PHA03247 2702 PPppptpepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAgpatpggparparpPTTAGPPA------PAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2155 WGGPVVSSQSTPESMLSGKSSYLPNsdPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHlGNFASSLSG 2234
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2235 GQMYGPGAPLGGAPLGGAPTAANFNRQHFSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSQDRKV 2314
Cdd:PHA03247 2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
                         410       420
                  ....*....|....*....|.
gi 568936357 2315 PVPIGTERSARIRQTGTSAPS 2335
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAG 2953
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
681-780 1.93e-07

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


:

Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   681 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 757
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 568936357   758 -KVERELQLKTQQQLKKQYLEVKA 780
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1742-2110 2.52e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1742 PAISSASTHKTIKNPVNNVRPGFPVSLPL--AYPPPQFAHALLAAQTFQQIRP-PRLPMTHFGGTFPPA-QSTWGPFPVR 1817
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPePAPHALVSATPLPPGpAAARQASPAL 2735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1818 PLSPA--RATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTASSSASAVPGTTSNGSPSSPSVRRQLFVTVVKTSNA 1895
Cdd:PHA03247 2736 PAAPAppAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1896 TTTTVTTTASNNSTAPTNATypmPTAkehypvsspsspspPAQPGGVSRNSPLDCGSASPNkGASASEQEASSPPVVEPA 1975
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQ---PTA--------------PPPPPGPPPPSLPLGGSVAPG-GDVRRRPPSRSPAAKPAA 2877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1976 NSRPPHSSSSSGSSsghstqQQPPGSVPQePRPPLQ-------------QSQVPSPDVRMTVPPTATSSAPVAVPSTAPV 2042
Cdd:PHA03247 2878 PARPPVRRLARPAV------SRSTESFAL-PPDQPErppqpqappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPA 2950
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2043 TYPMPQ-----TQMGCSQPPKMEAPAIRPPSHA---------TAAPHKTPAPVQSSSASVLNVnHIKrphSVPSSVQLPS 2108
Cdd:PHA03247 2951 GAGEPSgavpqPWLGALVPGRVAVPRFRVPQPApsreapassTPPLTGHSLSRVSSWASSLAL-HEE---TDPPPVSLKQ 3026

                  ..
gi 568936357 2109 TL 2110
Cdd:PHA03247 3027 TL 3028
Ank_2 super family cl48147
Ankyrin repeats (3 copies);
962-1000 9.95e-04

Ankyrin repeats (3 copies);


The actual alignment was detected with superfamily member pfam12796:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 9.95e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568936357   962 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1000
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
692-895 3.29e-03

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 766
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  767 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLFTSVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 846
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357  847 QALPLATGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 895
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-553 7.26e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 7.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568936357  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 1.53e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568936357  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1277 1.92e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  989 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1068
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1069 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1148
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1149 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1228
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1229 KGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPL 1277
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1613-1683 9.21e-40

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 142.20  E-value: 9.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1683
Cdd:cd22502     1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
984-1247 6.50e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.97  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  984 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 1059
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1060 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 1135
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1136 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssRD--- 1208
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA------RNryg 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568936357 1209 -TALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLA 1247
Cdd:PHA03095  258 qTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
127-447 1.79e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  127 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 202
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  203 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 276
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  277 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 343
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  344 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 422
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 568936357  423 TA----LTLACCGGFLEVADFLIKAGADI 447
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-282 2.73e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 568936357   272 LLLENGAGINT 282
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-546 4.48e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 534
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 568936357   535 FLISKGANVNRT 546
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1109-1200 5.97e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1109 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1188
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 568936357  1189 RVLLDKGADVNA 1200
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
137-350 1.44e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  137 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 209
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  210 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 343
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 568936357  344 GAQVNMP 350
Cdd:PHA03100  288 GFYKNRK 294
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1614-1678 5.34e-17

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 5.34e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357  1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1678
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 5.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 568936357   601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
KH smart00322
K homology RNA-binding domain;
1616-1680 3.36e-12

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 63.47  E-value: 3.36e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357   1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
1953-2335 4.58e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 72.28  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1953 ASPNKGASASEQEASSPPVVePANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRP------------PLQQSQVPSPDV 2020
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAA-PDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPrapvddrgdprgPAPPSPLPPDTH 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2021 RMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPA-IRPPSHAT--AAPHKTPAPvQSSSASVLNVNHIKRP 2097
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrARRLGRAAqaSSPPQRPRR-RAARPTVGSLTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2098 HS---------VPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSA--------------PLPFGPFStlfennPTNAHAF 2154
Cdd:PHA03247 2702 PPppptpepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAgpatpggparparpPTTAGPPA------PAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2155 WGGPVVSSQSTPESMLSGKSSYLPNsdPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHlGNFASSLSG 2234
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2235 GQMYGPGAPLGGAPLGGAPTAANFNRQHFSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSQDRKV 2314
Cdd:PHA03247 2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
                         410       420
                  ....*....|....*....|.
gi 568936357 2315 PVPIGTERSARIRQTGTSAPS 2335
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAG 2953
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
452-630 2.22e-11

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: 69.27  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  452 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 525
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  526 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 591
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568936357  592 AKGGHTSVVCYLLDYpnnLLAAPPPDvtQLTPPSHDLNR 630
Cdd:cd22192   177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
972-1091 1.17e-08

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: 60.41  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  972 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 1037
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1038 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1091
Cdd:cd22192   170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1946-2335 1.31e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1946 SPLDcgSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVP 2025
Cdd:pfam03154  150 SPQD--NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAP 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2026 PTATSSAPVAVPSTAPVTYPmPQTQMGCSQPPKMEAP-AIRPPSHATAAPhKTPAPVQSSSAsvlNVNHIKRPHSVPSSV 2104
Cdd:pfam03154  228 HTLIQQTPTLHPQRLPSPHP-PLQPMTQPPPPSQVSPqPLPQPSLHGQMP-PMPHSLQTGPS---HMQHPVPPQPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2105 Q--------LPSTLSTQSACQNSVHPANKPVA----PNFSAPLPFGPFStLFENNPTNAHAFWGGPVVSSQSTPeSMLSG 2172
Cdd:pfam03154  303 QssqsqvppGPSPAAPGQSQQRIHTPPSQSQLqsqqPPREQPLPPAPLS-MPHIKPPPTTPIPQLPNPQSHKHP-PHLSG 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2173 KSSYLPNSD--------PLHQSDTSKAPGFRPP----------LQRPAPSPSGIVNMDT--PYGSVTPSSTHLGNFASSL 2232
Cdd:pfam03154  381 PSPFQMNSNlppppalkPLSSLSTHHPPSAHPPplqlmpqsqqLPPPPAQPPVLTQSQSlpPPAASHPPTSGLHQVPSQS 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2233 SGGQM-YGPGAPLGGAPLGGAPTAANfnrqhfsplslltpcSSASNESPAQSVSSGVRAPSPAPSSVPLGS----EKPSS 2307
Cdd:pfam03154  461 PFPQHpFVPGGPPPITPPSGPPTSTS---------------SAMPGIQPPSSASVSSSGPVPAAVSCPLPPvqikEEALD 525
                          410       420
                   ....*....|....*....|....*...
gi 568936357  2308 VSQDRKVPVPigTERSARIRQTGTSAPS 2335
Cdd:pfam03154  526 EAEEPESPPP--PPRSPSPEPTVVNTPS 551
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
681-780 1.93e-07

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   681 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 757
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 568936357   758 -KVERELQLKTQQQLKKQYLEVKA 780
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
681-780 2.49e-07

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 52.92  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  681 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 756
Cdd:COG2825    30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                          90       100
                  ....*....|....*....|....*
gi 568936357  757 -QKVERELQLKTQQQLKKQYLEVKA 780
Cdd:COG2825   103 qQEAQQDLQKRQQELLQPILEKIQK 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
125-308 2.64e-07

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: 56.17  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 198
Cdd:cd22192    21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  199 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 260
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568936357  261 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 308
Cdd:cd22192   180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
521-625 6.48e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  521 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 600
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 568936357  601 CYLLDYPN---NLLAAPPPDVTQLTPPS 625
Cdd:PTZ00322  165 QLLSRHSQchfELGANAKPDSFTGKPPS 192
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
956-1192 1.03e-06

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: 54.32  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   956 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1032
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1033 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1098
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1099 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1151
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 568936357  1152 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1192
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
692-774 9.68e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 9.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEELNKTREEQIQKKQKILEELQK-VERELQLKTQQ 769
Cdd:TIGR04523  359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKLQQEKELLEKeIERLKETIIKN 438
                           90
                   ....*....|
gi 568936357   770 Q-----LKKQ 774
Cdd:TIGR04523  439 NseikdLTNQ 448
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
386-415 1.20e-05

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: 44.12  E-value: 1.20e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568936357    386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
691-773 2.33e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  691 PESIVEEAQGKLTELEQRIKEAIEKNAQLQ-SLE--LAHADQLtkekIEELNKTREEQIQKKQKILEELQKVERELQLKT 767
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEELErELEqkAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA 575

                  ....*.
gi 568936357  768 QQQLKK 773
Cdd:PRK00409  576 QQAIKE 581
PHA03247 PHA03247
large tegument protein UL36; Provisional
1742-2110 2.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1742 PAISSASTHKTIKNPVNNVRPGFPVSLPL--AYPPPQFAHALLAAQTFQQIRP-PRLPMTHFGGTFPPA-QSTWGPFPVR 1817
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPePAPHALVSATPLPPGpAAARQASPAL 2735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1818 PLSPA--RATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTASSSASAVPGTTSNGSPSSPSVRRQLFVTVVKTSNA 1895
Cdd:PHA03247 2736 PAAPAppAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1896 TTTTVTTTASNNSTAPTNATypmPTAkehypvsspsspspPAQPGGVSRNSPLDCGSASPNkGASASEQEASSPPVVEPA 1975
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQ---PTA--------------PPPPPGPPPPSLPLGGSVAPG-GDVRRRPPSRSPAAKPAA 2877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1976 NSRPPHSSSSSGSSsghstqQQPPGSVPQePRPPLQ-------------QSQVPSPDVRMTVPPTATSSAPVAVPSTAPV 2042
Cdd:PHA03247 2878 PARPPVRRLARPAV------SRSTESFAL-PPDQPErppqpqappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPA 2950
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2043 TYPMPQ-----TQMGCSQPPKMEAPAIRPPSHA---------TAAPHKTPAPVQSSSASVLNVnHIKrphSVPSSVQLPS 2108
Cdd:PHA03247 2951 GAGEPSgavpqPWLGALVPGRVAVPRFRVPQPApsreapassTPPLTGHSLSRVSSWASSLAL-HEE---TDPPPVSLKQ 3026

                  ..
gi 568936357 2109 TL 2110
Cdd:PHA03247 3027 TL 3028
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
123-376 2.99e-05

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: 49.69  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   123 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 199
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   200 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 277
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   278 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 328
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568936357   329 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 376
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
228-381 5.18e-05

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: 48.54  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   228 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 302
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   303 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 357
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 568936357   358 LTLAACGGHVELAALLIERGASLE 381
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
681-773 7.65e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.88  E-value: 7.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357    681 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 756
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 568936357    757 QKV-ERELQLKTQQQLKK 773
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1105-1133 7.76e-05

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: 41.80  E-value: 7.76e-05
                            10        20
                    ....*....|....*....|....*....
gi 568936357   1105 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1133
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
221-249 1.93e-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: 40.65  E-value: 1.93e-04
                            10        20
                    ....*....|....*....|....*....
gi 568936357    221 GNTALTYACAGGYVDVVKVLLESGASIED 249
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
2013-2316 2.02e-04

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 46.96  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2013 SQVPSPDVRMTVPPTATSSAPvavPSTAPVTYPMPQTQMGCSQP--PKMEAPAIRPPSHATAAPHKTP------------ 2078
Cdd:COG5665   253 EEKSSQQPKSQPTSPSGGTTP---PSTNQLTTSNTPTSTAKAQPqpPTKKQPAKEPPSDTASGNPSAPsvlinsdsptse 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2079 APVQSSSASVLNVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGPFSTLFE----NNPTNAHAF 2154
Cdd:COG5665   330 DPATASVPTTEETTAFTTPSSVPSTPAEKDTPATDLATPVSPTPPETSVDKKVSPDSATSSTKSEKEggtaSSPMPPNIA 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2155 WGgpvVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPL-----QRPAPSPSGIVNMDTPYGSVTPSSTHLGNFA 2229
Cdd:COG5665   410 IG---AKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSVRTEAspsagSDLEPENTTLRDPAPNAIPPPEDPSTIGRLS 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2230 SSLSGGQMYGPGAPLGGAPLGGAPTAANFNRQHFSPlslltpcssASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVS 2309
Cdd:COG5665   487 SGDKLANETGPPVIRRDSTPSSTADQSIVGVLAFGL---------DQRTQAEISVEAASRSNPLLNSQVKSFPLGKRSEG 557

                  ....*..
gi 568936357 2310 QDRKVPV 2316
Cdd:COG5665   558 AKGKTQT 564
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
709-774 3.85e-04

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


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 40.71  E-value: 3.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  709 IKEaiEKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 774
Cdd:cd22249     7 IRE--EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1613-1689 4.22e-04

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 45.77  E-value: 4.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1689
Cdd:COG1185   549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1613-1689 5.21e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.43  E-value: 5.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1689
Cdd:PRK11824  554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
Ank_2 pfam12796
Ankyrin repeats (3 copies);
962-1000 9.95e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 9.95e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568936357   962 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1000
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
969-997 1.24e-03

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: 38.34  E-value: 1.24e-03
                            10        20
                    ....*....|....*....|....*....
gi 568936357    969 NHDTALTLACAGGHEELVQTLLERGASIE 997
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
692-895 3.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 766
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  767 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLFTSVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 846
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357  847 QALPLATGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 895
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-553 7.26e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 7.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568936357  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
301-613 1.29e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.80  E-value: 1.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  301 LEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 380
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  381 EEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcsTPLMEAAQ 460
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-------------------------------TPLHLAAY 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  461 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKG 540
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357  541 ANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLAA 613
Cdd:COG0666   210 ADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 1.53e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568936357  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
989-1277 1.92e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  989 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1068
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1069 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1148
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1149 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1228
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1229 KGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPL 1277
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
234-521 2.00e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 2.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  234 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEMVRFLLEAGAD 313
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG-ALLLLAAALAGDLLVALLLLAAGAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  314 QEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLME 393
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  394 AAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYL 470
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgkTALDLAAENGNLEIVKLL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568936357  471 LAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL 521
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
201-488 1.64e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.25  E-value: 1.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  201 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGI 280
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  281 NThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 360
Cdd:COG0666    81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  361 AACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFL 440
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568936357  441 IKAGADIELGC---STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTAL 488
Cdd:COG0666   239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
952-1200 1.54e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  952 AMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1031
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1032 QSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLML 1111
Cdd:COG0666   116 RDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1112 AAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVL 1191
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

                  ....*....
gi 568936357 1192 LDKGADVNA 1200
Cdd:COG0666   272 LLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
368-621 4.76e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.01  E-value: 4.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  368 ELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADI 447
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  448 EL---GCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKA 524
Cdd:COG0666    81 NAkddGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  525 ARAGHVCTVQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 604
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250
                  ....*....|....*..
gi 568936357  605 DYPNNLLAAPPPDVTQL 621
Cdd:COG0666   240 EAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
953-1244 5.44e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.62  E-value: 5.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  953 MLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1032
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1033 SERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLA 1112
Cdd:COG0666    84 DDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1113 AMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1192
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1193 DKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPL 1244
Cdd:COG0666   240 EAGADLNAK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
40-325 1.33e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   40 LLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQ 119
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  120 SDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGG 199
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  200 HVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAG 279
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568936357  280 INtHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 325
Cdd:COG0666   245 LN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1085-1294 2.01e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1085 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKAN 1164
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1165 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPL 1244
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936357 1245 WLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1294
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1613-1683 9.21e-40

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 142.20  E-value: 9.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1683
Cdd:cd22502     1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
1613-1694 2.36e-37

type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells.


Pssm-ID: 411931  Cd Length: 83  Bit Score: 136.03  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIP 1692
Cdd:cd22503     1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80

                  ..
gi 568936357 1693 KN 1694
Cdd:cd22503    81 RN 82
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
1613-1683 1.09e-36

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 133.49  E-value: 1.09e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1683
Cdd:cd22404     1 KSKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDKQKGEQGDRRITIKGSADATRQAAQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
984-1247 6.50e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.97  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  984 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 1059
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1060 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 1135
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1136 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssRD--- 1208
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA------RNryg 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568936357 1209 -TALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLA 1247
Cdd:PHA03095  258 qTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1039-1325 1.45e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 112.07  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1039 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1113
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1114 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1189
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1190 VLLDKGADVNappvpssrdtaltiAADKghykfCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAA 1269
Cdd:PHA03100  161 LLIDKGVDIN--------------AKNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 1270 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1325
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
127-447 1.79e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  127 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 202
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  203 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 276
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  277 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 343
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  344 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 422
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 568936357  423 TA----LTLACCGGFLEVADFLIKAGADI 447
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-282 2.73e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 568936357   272 LLLENGAGINT 282
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-546 4.48e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 534
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 568936357   535 FLISKGANVNRT 546
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
334-512 6.91e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  334 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 406
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  407 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 465
Cdd:PHA03100  128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568936357  466 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 512
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-416 5.69e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   325 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASleEVNDEGYTPLMEAAREGHEEMVA 404
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 568936357   405 LLLGQGANINAQ 416
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1109-1200 5.97e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1109 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1188
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 568936357  1189 RVLLDKGADVNA 1200
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
283-591 7.73e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.64  E-value: 7.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  283 HSNEFKESAL---TLACYKGHLEMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 355
Cdd:PHA03095    6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  356 SPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAAR--EGHEEMVALLLGQGANINAqTEETQETALtlaccgg 432
Cdd:PHA03095   85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNA-LDLYGMTPL------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  433 flevADFLIKAGADIELgcstplmeaaqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 510
Cdd:PHA03095  157 ----AVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  511 EHESEGGRTPLMKAArAGHVCT---VQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 587
Cdd:PHA03095  216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                  ....
gi 568936357  588 LIEA 591
Cdd:PHA03095  294 LSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
125-510 1.21e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDV--NAVRKLLIEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVEDRGIKGdITPLMAAANGGHVK 202
Cdd:PHA02876  125 LKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADVNAKDIYC-ITPIHYAAERGNAK 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  203 IVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIedhNENGHTpLMEAGSAGHVEVARLLLENGAGINT 282
Cdd:PHA02876  193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDLETSLLLYDAGFSVNS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  283 hSNEFKESALTLACYKGHL-EMVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGAQVNMPADSFESPLTL 360
Cdd:PHA02876  269 -IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQ 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  361 AAC-GGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGG--FLEVA 437
Cdd:PHA02876  348 ASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTnpYMSVK 426
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357  438 DfLIKAGADIELG---CSTPLMEAAQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTDVADVLLQAGADL 510
Cdd:PHA02876  427 T-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-317 4.56e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 4.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   225 LTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENgagINTHSNEFKESALTLACYKGHLEMV 304
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 568936357   305 RFLLEAGADQEHK 317
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
258-348 7.79e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 7.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   258 LMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 337
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 568936357   338 RLLLDSGAQVN 348
Cdd:pfam12796   78 KLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
176-415 1.07e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  176 MHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYV-----DVVKVLLESGASIEDH 250
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  251 NENGHTPLMEAGSA--GHVEVARLLLENGAGINTHSNEFKES-ALTLACYKGHLEMVRFLLEAGADQEHKTDemhtalme 327
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  328 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 407
Cdd:PHA03100  175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                  ....*...
gi 568936357  408 GQGANINA 415
Cdd:PHA03100  246 NNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1074-1168 2.43e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1074 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKLLLDMgsdINAQIETNRNTALTLACFQGRTE 1153
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 568936357  1154 VVSLLLDRKANVEHR 1168
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
983-1167 2.80e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  983 EELVQTLLERGASIEHRDKKGFTPLILAATAGHV-----GVVEILLDNGADIEAQSERTkDTPLSLACSGGRQ--EVVEL 1055
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKKSNsySIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1056 LLARGANKEHRNVSDYTPLSLAASGGYV--NIIKILLNAGAEINSRT--------GSKL------GISPLMLAAMNGHTA 1119
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsyGVPInikdvyGFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568936357 1120 AVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVVSLLLDRKANVEH 1167
Cdd:PHA03100  207 FVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
391-480 6.25e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 6.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   391 LMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGGFLEVADFLI-KAGADIELGCSTPLMEAAQEGHLELVKY 469
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|.
gi 568936357   470 LLAAGANVHAT 480
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
488-580 7.16e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 7.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   488 LTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKgANVNRTtaNNDHTVLSLACAGGHLAVV 567
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK--DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 568936357   568 ELLLAHGADPTHR 580
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1041-1134 1.68e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1041 LSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHTAA 1120
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 568936357  1121 VKLLLDMGSDINAQ 1134
Cdd:pfam12796   77 VKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
984-1137 1.74e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  984 ELVQTLLERGASIEHRDKKGFTPLILAATA--GHVGVVEILLDNGADIEAQSERTKdTPLSLACSGGRQ--EVVELLLAR 1059
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIdlKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1060 GA--NKEHR--------------NVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKL 1123
Cdd:PHA03100  166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|....
gi 568936357 1124 LLDMGSDINAQIET 1137
Cdd:PHA03100  244 LLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
199-521 1.91e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  199 GHVKIVKLLLAHKAD-VNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENG 277
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  278 agINThsnefkeSALTLACYKGhlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02874   92 --VDT-------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQteetqetaltlaCCGGFleva 437
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  438 dflikagadielgcsTPLMEAAQegHLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHE 513
Cdd:PHA02874  225 ---------------TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIK 284

                  ....*...
gi 568936357  514 SEGGRTPL 521
Cdd:PHA02874  285 DNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
974-1067 2.05e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   974 LTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNgADIEAQSErtKDTPLSLACSGGRQEVV 1053
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 568936357  1054 ELLLARGANKEHRN 1067
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
233-539 2.20e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  233 YVDVVKVLLESGASIEDHNENGHTPL---MEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLE 309
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  310 AGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGASLE 381
Cdd:PHA03095  106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  382 EVNDEGYTPLmeaaregheemvalllgqgaNINAQTEETQETaltlaccggfleVADFLIKAGAD---IELGCSTPLMEA 458
Cdd:PHA03095  182 AVDDRFRSLL--------------------HHHLQSFKPRAR------------IVRELIRAGCDpaaTDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  459 AQEGHLE--LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 536
Cdd:PHA03095  230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                  ...
gi 568936357  537 ISK 539
Cdd:PHA03095  310 LAK 312
PHA02876 PHA02876
ankyrin repeat protein; Provisional
985-1281 4.13e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  985 LVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIE------------AQSERTKDT------------- 1039
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDSKNIDTikaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1040 -PLSL--ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMN 1115
Cdd:PHA02876  240 nDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKN 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1116 GH-TAAVKLLLDMGSDINAQiETNRNTALTLACFQGR-TEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLD 1193
Cdd:PHA02876  318 GYdTENIRTLIMLGADVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1194 KGADVNAppVPSSRDTALTIA-ADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAA-NGGHLDVVQLLVQATADVDAADN 1271
Cdd:PHA02876  397 YGADIEA--LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINI 474
                         330
                  ....*....|
gi 568936357 1272 RKITPLMAAF 1281
Cdd:PHA02876  475 QNQYPLLIAL 484
Ank_2 pfam12796
Ankyrin repeats (3 copies);
358-449 5.42e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 5.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLgQGANINAQTEetQETALTLACCGGFLEVA 437
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 568936357   438 DFLIKAGADIEL 449
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1211-1294 6.33e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 6.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1211 LTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQaTADVDAADNRKiTPLMAAFRKGHVKVVR 1290
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....
gi 568936357  1291 YLVK 1294
Cdd:pfam12796   79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
236-606 1.12e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.20  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  236 VVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEfKESALTLACYKGHLEMVRFLLeagaDQE 315
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  316 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGASLEEVNDEGYTPLMEA 394
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  395 AREGHE-EMVALLLGQGANINAqteetqetaltlaccggflevADFLIkagadielgcSTPLMEAAQ-EGHLELVKYLLA 472
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  473 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-VCTVQFLISKGANVNrtTANND 551
Cdd:PHA02876  364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  552 -HTVLSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTSVVCYLLDY 606
Cdd:PHA02876  442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
137-350 1.44e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  137 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 209
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  210 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 343
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 568936357  344 GAQVNMP 350
Cdd:PHA03100  288 GFYKNRK 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
960-1203 5.52e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 5.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  960 IDIDAqTESNHDTAL-TLACAGGHEELVQTLLERGASIEHRDKKGFTPL--ILAATAGHVGVVEILLDNGADIEAQSERT 1036
Cdd:PHA03095   74 ADVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1037 KdTPLS--------------LACSGG-----------------------RQEVVELLLARGANKEHRNVSDYTPLSLAAS 1079
Cdd:PHA03095  153 M-TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1080 GGYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrNTALTLACFQGRTEVVSL 1157
Cdd:PHA03095  232 GSSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRA 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1158 LLDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1203
Cdd:PHA03095  309 ALAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
PHA03095 PHA03095
ankyrin-like protein; Provisional
401-614 1.45e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.54  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  401 EMVALLLGQGANINaQTEETQETALT--LAC-CGGFLEVADFLIKAGADIEL----GCsTPL---MEAAQEghLELVKYL 470
Cdd:PHA03095   28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVNApercGF-TPLhlyLYNATT--LDVIKLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  471 LAAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHVCTVQFLISKGANVnR 545
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADV-Y 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  546 TTANNDHTVLSLacaggHL-------AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTSVVCYLL------DYPNNL 610
Cdd:PHA03095  182 AVDDRFRSLLHH-----HLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLiagisiNARNRY 256

                  ....
gi 568936357  611 LAAP 614
Cdd:PHA03095  257 GQTP 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1143-1237 1.54e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1143 LTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1222
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 568936357  1223 CELLIGKGAHIDVRN 1237
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1013-1342 1.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.10  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1013 AGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNA 1092
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1093 GAEinsrtgsklgISPLMLAAMNGHTaaVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTG 1172
Cdd:PHA02874   91 GVD----------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1173 LTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLA----- 1247
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnr 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1248 ----------------ANGG-----------HLDVVQLLVQATADVDAADNRKITPLMAAFRK-GHVKVVR------YLV 1293
Cdd:PHA02874  236 saiellinnasindqdIDGStplhhainppcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLI 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1294 KEVNQFPsDSECMRYIATITDKEMLKKCHLCMESIVQAKdRQAAEANKN 1342
Cdd:PHA02874  316 KEADKLK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK-KTKCGCDKN 362
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1176-1270 1.78e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 1.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1176 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIgkgAHIDVRNK-KGNTPLWLAANGGHLD 1254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 568936357  1255 VVQLLVQATADVDAAD 1270
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
972-1164 2.15e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  972 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQE 1051
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1052 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHTAAVKLLLDMGSDI 1131
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568936357 1132 NAqieTNRNTALTLACF---QGRTEVVSLLLDRKAN 1164
Cdd:PHA02875  195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-217 2.30e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGikgdITPLMAAANGGHVKI 203
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG----RTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 568936357   204 VKLLLAHKADVNAQ 217
Cdd:pfam12796   77 VKLLLEKGADINVK 90
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1614-1678 5.34e-17

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 5.34e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357  1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1678
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
1615-1677 8.78e-16

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 73.49  E-value: 8.78e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLIN 1677
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
192-360 1.18e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  272 LLLENGAGINTHSNefkESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVN-MP 350
Cdd:PLN03192  609 ILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkAN 685
                         170
                  ....*....|
gi 568936357  351 ADSFESPLTL 360
Cdd:PLN03192  686 TDDDFSPTEL 695
PHA02875 PHA02875
ankyrin repeat protein; Provisional
224-446 4.45e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 4.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  224 ALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEM 303
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  304 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLE 381
Cdd:PHA02875   84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357  382 EVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGAD 446
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 5.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 568936357   601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
1153-1294 5.29e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.45  E-value: 5.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1153 EVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC------ 1223
Cdd:PHA03095   28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnattld 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1224 --ELLIGKGAHIDVRNKKGNTPL--WLAANGGHLDVVQLLVQATADVDAADNRKITPLmAAFRKGH---VKVVRYLVK 1294
Cdd:PHA03095   99 viKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
133-329 8.23e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 8.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  133 DVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKA 212
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  213 DVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESAL 292
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568936357  293 TLACYKGHLEMVRFLLEAGADQEHKT---DEMHTALMEAC 329
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
324-576 1.11e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  324 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAsLEEVNDEGY-TPLMEAAREGHEEM 402
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  403 VALLLGQGANINaqteetqetaltlaccggflevaDFLIKAGadielgcSTPLMEAAQEGHLELVKYLLAAGANVHATTA 482
Cdd:PHA02875   84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  483 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGG 562
Cdd:PHA02875  134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
                         250
                  ....*....|....
gi 568936357  563 HLAVVELLLAHGAD 576
Cdd:PHA02875  214 KIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
365-591 2.43e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  365 GHVELAALLIE-RGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTlACCGGFLEVADFLIKA 443
Cdd:PHA02874   12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  444 GADIELgCSTPLMEAaqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 523
Cdd:PHA02874   91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  524 AARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 591
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1039-1231 1.48e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.41  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1039 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHT 1118
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1119 AAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1198
Cdd:PHA02875  116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568936357 1199 N----APPVpssrdTALTIAADKGHYKFCELLIGKGA 1231
Cdd:PHA02875  195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
984-1283 1.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  984 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVGVVEILLDNGADIEAQSERTkdtpLSLACSGGRQEVVELLLARGAN 1062
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA----IKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1063 KEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrN 1140
Cdd:PHA02878  127 NIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-N 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1141 TALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVLLDKGADVNAppvpssRDTALTIAAdk 1217
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYILGLTA-- 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357 1218 ghykfcelligkgAHIDVRNKkgntplwlaangghlDVVQLLVQATADVDAADNRKITPLMAAFRK 1283
Cdd:PHA02878  273 -------------LHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
158-378 2.81e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  158 LCLACSAGYYELAQVLLAMHANvEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 237
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGIN-PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  238 KVLLESGASIED-HNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH 316
Cdd:PHA02875   85 EELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  317 KTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAdsfESPLTLAACGG----HVELAALLIERGA 378
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG---KNGCVAALCYAiennKIDIVRLFIKRGA 226
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
1616-1680 2.92e-13

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4.


Pssm-ID: 411890 [Multi-domain]  Cd Length: 66  Bit Score: 66.50  E-value: 2.92e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22462     2 EILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLIEAFI 66
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1614-1679 3.18e-13

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 66.48  E-value: 3.18e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINAL 1679
Cdd:cd22439     3 TQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
199-427 5.08e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  199 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGAsIEDHNENG-HTPLMEAGSAGHVEVARLLLENG 277
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  278 AGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02875   92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357  358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHE-EMVALLLGQGANINAQTEETQETALTL 427
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTIL 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1044-1265 5.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.49  E-value: 5.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1044 ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHTAAVK 1122
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1123 LLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1202
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 1203 VPSSrdTALTIAADKGHYKFCELLIGKGAHIDVRNKKGN-TPLWLAANGGHLDVVQLLVQATAD 1265
Cdd:PHA02875  166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
956-1032 5.75e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 5.75e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   956 IYPAIDIDAQTEsNHDTALTLACAGGHEELVQTLLERgASIEHRDkKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1032
Cdd:pfam12796   17 LENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
336-571 2.49e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  336 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGAN--I 413
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  414 NAQTEETQETALTLACCGGFLEVADFLIKagadielgcsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACE 493
Cdd:PHA02874   97 LPIPCIEKDMIKTILDCGIDVNIKDAELK----------TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  494 NGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHlAVVELLL 571
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1018-1192 2.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1018 VVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1097
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1098 SRtgSKLGISPLMLAAMNGHTAAV-KLLLDMGSDINAQIETNRNTALTLACFQGRteVVSLLLDRKANVEHRAKTGLTPL 1176
Cdd:PHA02878  229 AR--DKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPL 304
                         170
                  ....*....|....*..
gi 568936357 1177 MEAASGGYA-EVGRVLL 1192
Cdd:PHA02878  305 SSAVKQYLCiNIGRILI 321
PHA02878 PHA02878
ankyrin repeat protein; Provisional
123-313 3.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  123 RSLAEACSEGDVNAVRKLLIegrsvNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGIKGDITPLMAAAN 197
Cdd:PHA02878  103 VAIKDAFNNRNVEIFKIILT-----NRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  198 GGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL-MEAGSAGHVEVARLLLEN 276
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568936357  277 GAGINTHSNEFKESALTLACYKGhlEMVRFLLEAGAD 313
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
KH smart00322
K homology RNA-binding domain;
1616-1680 3.36e-12

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 63.47  E-value: 3.36e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357   1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
1953-2335 4.58e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 72.28  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1953 ASPNKGASASEQEASSPPVVePANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRP------------PLQQSQVPSPDV 2020
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAA-PDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPrapvddrgdprgPAPPSPLPPDTH 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2021 RMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPA-IRPPSHAT--AAPHKTPAPvQSSSASVLNVNHIKRP 2097
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrARRLGRAAqaSSPPQRPRR-RAARPTVGSLTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2098 HS---------VPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSA--------------PLPFGPFStlfennPTNAHAF 2154
Cdd:PHA03247 2702 PPppptpepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAgpatpggparparpPTTAGPPA------PAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2155 WGGPVVSSQSTPESMLSGKSSYLPNsdPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHlGNFASSLSG 2234
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2235 GQMYGPGAPLGGAPLGGAPTAANFNRQHFSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSQDRKV 2314
Cdd:PHA03247 2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
                         410       420
                  ....*....|....*....|.
gi 568936357 2315 PVPIGTERSARIRQTGTSAPS 2335
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAG 2953
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1077-1294 4.80e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 4.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1077 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVS 1156
Cdd:PHA02875    9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1157 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIGKGAHID 1234
Cdd:PHA02875   86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1235 VRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRK-ITPLMAAFRKGHVKVVRYLVK 1294
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
926-1198 4.81e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  926 NTPTHSIAasvsqpQTPtpspiiSPSAMLP--IYPAIDIDAQTESNhDTALTLACAGGHE-ELVQTLLERGASIEHRDKK 1002
Cdd:PHA02876  274 NTPLHHAS------QAP------SLSRLVPklLERGADVNAKNIKG-ETPLYLMAKNGYDtENIRTLIMLGADVNAADRL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1003 GFTPLILAATaghvgvveilLDngadieaqseRTKDTPLSlacsggrqevvelLLARGANKEHRNVSDYTPLSLAASGGY 1082
Cdd:PHA02876  341 YITPLHQAST----------LD----------RNKDIVIT-------------LLELGANVNARDYCDKTPIHYAAVRNN 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1083 VNIIKILLNAGAEINSRTgSKLGIS-PLMLAAMNGHTaAVKLLLDMGSDINAQiETNRNTALTLACFQG-RTEVVSLLLD 1160
Cdd:PHA02876  388 VVIINTLLDYGADIEALS-QKIGTAlHFALCGTNPYM-SVKTLIDRGANVNSK-NKDLSTPLHYACKKNcKLDVIEMLLD 464
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568936357 1161 RKANVEHRAKTGLTPLMEAAsgGYAEVGRVLLDKGADV 1198
Cdd:PHA02876  465 NGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
334-514 5.51e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  334 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGASLEEVND-EGYTPLMEAAREGHEEMVALLLGQGAN 412
Cdd:PLN03192  507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  413 INAQtEETQETALTLACCGGFLEVADFLIK--------AGADIelgcstpLMEAAQEGHLELVKYLLAAGANVHATTATG 484
Cdd:PLN03192  584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
                         170       180       190
                  ....*....|....*....|....*....|
gi 568936357  485 DTALTYACENGHTDVADVLLQAGADLEHES 514
Cdd:PLN03192  656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-241 5.69e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 5.69e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357   190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLL 241
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
369-636 6.58e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 6.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  369 LAALLIERGASLEE---VNDEGYTPLMEAAREGHEEMVALLLGQ--GANINAQTEETQET-ALTLACCG--GFLEVadfL 440
Cdd:PLN03192  468 LSQLLRLKTSTLIEamqTRQEDNVVILKNFLQHHKELHDLNVGDllGDNGGEHDDPNMASnLLTVASTGnaALLEE---L 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  441 IKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAgADLEHESEGG 517
Cdd:PLN03192  545 LKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAG 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  518 RTpLMKAARAGHVCTVQFLISKGANVNrttaNNDH---TVLSLACAGGHLAVVELLLAHGADPTHRLKD---GSTMLIEA 591
Cdd:PLN03192  624 DL-LCTAAKRNDLTAMKELLKQGLNVD----SEDHqgaTALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELREL 698
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357  592 AK----GGHTSVVCYLLDYPNNLLAAPPPDVTQLTPPSHDLNRAPRVPV 636
Cdd:PLN03192  699 LQkrelGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI 747
Ank_4 pfam13637
Ankyrin repeats (many copies);
451-504 1.13e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 1.13e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   451 CSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 504
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
1614-1683 1.27e-11

third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 62.34  E-value: 1.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1683
Cdd:cd22434     3 TTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIITITGTQDQIQNAQYLLQNSVKQY 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
452-630 2.22e-11

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: 69.27  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  452 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 525
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  526 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 591
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568936357  592 AKGGHTSVVCYLLDYpnnLLAAPPPDvtQLTPPSHDLNR 630
Cdd:cd22192   177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
PHA02878 PHA02878
ankyrin repeat protein; Provisional
234-526 2.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  234 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLengAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGAD 313
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  314 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTP 390
Cdd:PHA02878  127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  391 LMEAAREGHEEMVALLLGQGANINAQTEetqetaltlacCGgflevadflikagadielgcSTPL-MEAAQEGHLELVKY 469
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  470 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 526
Cdd:PHA02878  254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1138-1294 5.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 5.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1138 NRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1215
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1216 DKGHYKFCELLIGKGAHI-DVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1294
Cdd:PHA02875   77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
PHA02878 PHA02878
ankyrin repeat protein; Provisional
191-447 6.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 6.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  191 PLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgaSIEDHNENGHTPLMEAGSAGHVEVA 270
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  271 RLLLengagINTHSNEfKESALTLACYKGH-----LEMVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 344
Cdd:PHA02878  118 KIIL-----TNRYKNI-QTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  345 AQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL-MEAAREGHEEMVALLLGQGANINAQTEETQET 423
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
                         250       260
                  ....*....|....*....|....
gi 568936357  424 ALTLACCGGflEVADFLIKAGADI 447
Cdd:PHA02878  272 ALHSSIKSE--RKLKLLLEYGADI 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
256-471 9.98e-11

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: 67.35  E-value: 9.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  256 TPLMEAGSAGHVE-VARLLLENGAGINTHSnEFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMH---TALMEAC 329
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  330 MDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL---- 391
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  392 MEAAREGHEEMVALLLGQGANINAQTEETQETALTLaccggflevadflikagadielgcsTPLMEAAQEGHLELVKYLL 471
Cdd:cd22192   178 LQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGL-------------------------TPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1244-1298 1.36e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 1.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568936357  1244 LWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQ 1298
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
1207-1260 2.95e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 2.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357  1207 RDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1260
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
116-294 3.86e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  116 NAGQSDNRSLAE----ACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTP 191
Cdd:PLN03192  516 NGGEHDDPNMASnlltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TA 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  192 LMAAANGGHVKIVKLLLAHKADVNAQssTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PLN03192  595 LWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180
                  ....*....|....*....|....
gi 568936357  272 LLLENGAGInTHSNEFKE-SALTL 294
Cdd:PLN03192  673 LLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
970-1023 4.54e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 4.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   970 HDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1023
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
190-316 6.20e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgASIEDHNENGHTpLMEAGSAGHVEV 269
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTA 637
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568936357  270 ARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLLEAGADQEH 316
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
132-253 6.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  132 GDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR-------GIKGDI------TPLMA 194
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsyGVPINIkdvygfTPLHY 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  195 AANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNEN 253
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1624-1678 6.85e-10

second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 57.24  E-value: 6.85e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1624 ISRVIGRGGCNINAIRECTGAHIDIDKQKDKT---GDRIITIRGGTESTRQATQLINA 1678
Cdd:cd22401    11 CGRLIGKDGRNIKKIMEDTNTKITISSLQDLTsynPERTITIKGSLEAMSEAESLISE 68
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1615-1676 8.62e-10

third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 56.82  E-value: 8.62e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd09031     3 IELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEfvpGTRNRKVTITGTPAAVQAAQYLI 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
1769-2297 9.43e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 9.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1769 PLAYPPP-QFAHALLAAQTFQQIRPPRLpMTHFGGTFPPAQSTWG----PFPVRPLSPARATNSPKPHMVPRHSNQnssg 1843
Cdd:PHA03247 2506 PDAPPAPsRLAPAILPDEPVGEPVHPRM-LTWIRGLEELASDDAGdpppPLPPAAPPAAPDRSVPPPRPAPRPSEP---- 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1844 sqvnSAGSLTSSPTTTASSSASAVPGTTSNGSPSSPSvrrqlfvtvvktsnattttvtttasnNSTAPTNATYPMPTA-- 1921
Cdd:PHA03247 2581 ----AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAP--------------------------PSPLPPDTHAPDPPPps 2630
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1922 KEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKGASASEQ--EASSPPvvepanSRPPHSSSSSGSSSGHSTQQQPP 1999
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRaaQASSPP------QRPRRRAARPTVGSLTSLADPPP 2703
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2000 GSVPQEPRPPLQQSQVPSPDVRMTV-----PPTATSSAPVAVPSTA-PVTYPMPQTQMGCSQPPKMEAPAIRPpshATAA 2073
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAArqaspALPAAPAPPAVPAGPAtPGGPARPARPPTTAGPPAPAPPAAPA---AGPP 2780
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2074 PHKTPAPVQSSSASVLNVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNfSAPLPFGPFSTlfeNNPTNAHA 2153
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPPP---SLPLGGSV 2856
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2154 FWGGPVV------SSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSthlgn 2227
Cdd:PHA03247 2857 APGGDVRrrppsrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP----- 2931
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 2228 faSSLSGGQMYGPGAPLGGAPLGGAPTAANFNRQ--HFSPLSL-----LTPCSSASNESPAQSVSSGVRAPSPAPSS 2297
Cdd:PHA03247 2932 --PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgALVPGRVavprfRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
Ank_4 pfam13637
Ankyrin repeats (many copies);
1240-1293 1.44e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357  1240 GNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYLV 1293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
555-608 1.58e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 1.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   555 LSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPN 608
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1615-1680 1.72e-09

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 56.19  E-value: 1.72e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKT--GDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22428     7 IEMKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGelPERVLLIQGNPVQAQRAEEAIHQII 74
PHA02874 PHA02874
ankyrin repeat protein; Provisional
125-285 1.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----------------AMHANVEDRGIKGD 188
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekDMIKTILDCGIDVN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  189 I------TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAG 262
Cdd:PHA02874  119 IkdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         170       180
                  ....*....|....*....|...
gi 568936357  263 SAGHVEVARLLLENGAGINTHSN 285
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCK 221
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1614-1678 2.01e-09

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411951  Cd Length: 68  Bit Score: 55.67  E-value: 2.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1678
Cdd:cd22523     3 SQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLITT 67
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
979-1057 2.09e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  979 AGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAqSERTKDTPLSLACSGGRQEVVELLL 1057
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
221-274 2.15e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   221 GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 274
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1615-1676 2.19e-09

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 55.54  E-value: 2.19e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22457     1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPhDETGERMFTITGTPEANDRALRLL 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1107-1270 2.21e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1107 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1186
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1187 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADV 1266
Cdd:PLN03192  606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                  ....
gi 568936357 1267 DAAD 1270
Cdd:PLN03192  682 DKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
254-308 2.21e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.21e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568936357   254 GHTPLMEAGSAGHVEVARLLLENGAGINtHSNEFKESALTLACYKGHLEMVRFLL 308
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
553-604 2.37e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357   553 TVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 604
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
484-537 2.37e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   484 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 537
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
125-397 2.61e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSA----GYYELAQVLLAMHANVEDRGIKgditplmAAANGGH 200
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIK-------DAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  201 VKIVKLLLAHKADVNAQSStgntaLTYACAGGYVD-----VVKVLLESGASIEDHNEN-GHTPLMEAGSAGHVEVARLLL 274
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTID-----LVYIDKKSKDDiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  275 ENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEA---CMDghVEVARLLLDSGAQVNmpA 351
Cdd:PHA02878  189 SYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVN--A 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568936357  352 DSFESPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAARE 397
Cdd:PHA02878  264 KSYILGLTALHSSIKSErKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1004-1282 2.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1004 FTPLILAATAGHVGVVEILLDNGADIEaQSERTKDTPLSLACSG----GRQEVVELLLARGANKEHRNVSDytplslAAS 1079
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKD------AFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1080 GGYVNIIKILLNAGAEiNSRTGSKLGISPLMLAAMNgHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLL 1159
Cdd:PHA02878  111 NRNVEIFKIILTNRYK-NIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1160 DRKANVEHRAKTGLTPLMEAASggyaevgrvlldkgadvnappvpssrdtaltiaadkgHY--KFCELLIGKGAHIDVRN 1237
Cdd:PHA02878  189 SYGANVNIPDKTNNSPLHHAVK-------------------------------------HYnkPIVHILLENGASTDARD 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1238 KKGNTPLWLAAngGHL---DVVQLLVQATADVDAADN-RKITPLMAAFR 1282
Cdd:PHA02878  232 KCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1614-1676 3.16e-09

second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one.


Pssm-ID: 411857 [Multi-domain]  Cd Length: 82  Bit Score: 55.80  E-value: 3.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGD--RIITIRGGTESTRQATQLI 1676
Cdd:cd22429     3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDlvRLITITGTKKEVDAAKSLI 67
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1063-1277 3.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1063 KEHR----NVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKlGISPLMLAAMNGHTAAVKLLLdmgSDINAQIETN 1138
Cdd:PHA02878   26 TENYstsaSLIPFIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHR-DLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1139 RNTALTLACFQGRTEVV-SLLLDRKANVEhraKTGLTPLMEAASGGY--AEVGRVLLDKGADVNAPPvPSSRDTALTIAA 1215
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIFkIILTNRYKNIQ---TIDLVYIDKKSKDDIieAEITKLLLSYGADINMKD-RHKGNTALHYAT 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1216 DKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPL 1277
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PHA02798 PHA02798
ankyrin-like protein; Provisional
201-418 4.89e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  201 VKIVKLLLAHKADVNAQSSTGNTALT--------YACAggyVDVVKVLLESGASIEDHNENGHTP---LMEAGSAGHVEV 269
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnikdYKHM---LDIVKILIENGADINKKNSDGETPlycLLSNGYINNLEI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  270 ARLLLENGAGINTHSNeFKESALTLACYKGH---LEMVRFLLEAGAD-----QEHKTDEMHTALME--ACMDghVEVARL 339
Cdd:PHA02798  128 LLFMIENGADTTLLDK-DGFTMLQVYLQSNHhidIEIIKLLLEKGVDinthnNKEKYDTLHCYFKYniDRID--ADILKL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  340 LLDSGAQVNMPADSFESPL-----TLAACGGHVELAAL-LIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANI 413
Cdd:PHA02798  205 FVDNGFIINKENKSHKKKFmeylnSLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDI 284

                  ....*
gi 568936357  414 NAQTE 418
Cdd:PHA02798  285 NIITE 289
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
1613-1683 4.98e-09

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 54.79  E-value: 4.98e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDP 1683
Cdd:cd02393     4 RITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED------DGTVTIFATDkESAEAAKAMIEDIVAEP 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
1773-2233 5.59e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1773 PPPQFAHALLAAQTFQQIRPPRL------PMTHFGGTFP--PAQSTWGPFPVRPLSPARATNSPKP----HMVPRHSNQN 1840
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPaprpsePAVTSRARRPdaPPQSARPRAPVDDRGDPRGPAPPSPlppdTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1841 SSGSQVNSAGSLTSSPTTTASSSASAVPG-------TTSNGSPSSPSV------RRQLFVTVVKTSNATTTTVTTTASNN 1907
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSppqrprRRAARPTVGSLTSLADPPPPPPTPEP 2710
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1908 STAPTNATYPMPTAKEHYPVSSPSSPSPPAQPGgVSRNSPLDCGSASPNKGASASEQEASSPPVVePANSRPPHSSSSSG 1987
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAA-PAAGPPRRLTRPAV 2788
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1988 SSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEApAIRPP 2067
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV-RRRPP 2867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2068 SHATAAPHKTPA--PVQSSSASVLNvnhiKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGPfstlfe 2145
Cdd:PHA03247 2868 SRSPAAKPAAPArpPVRRLARPAVS----RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP------ 2937
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2146 nNPTNAHAFWGGPVVSSQSTPESMLSGKSSYLPNSDPLHQSdtsKAPGFRPPLQRPAPSPSgivnmdTPYGSVTPSsthL 2225
Cdd:PHA03247 2938 -RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF---RVPQPAPSREAPASSTP------PLTGHSLSR---V 3004

                  ....*...
gi 568936357 2226 GNFASSLS 2233
Cdd:PHA03247 3005 SSWASSLA 3012
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1616-1676 9.86e-09

second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 53.78  E-value: 9.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDK--TGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22436     4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPESinLQERVVTVTGEPEANRKAVSLI 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
356-407 1.03e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357   356 SPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 407
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-374 1.07e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.07e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357   321 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 374
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
972-1091 1.17e-08

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: 60.41  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  972 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 1037
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1038 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1091
Cdd:cd22192   170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1946-2335 1.31e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1946 SPLDcgSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVP 2025
Cdd:pfam03154  150 SPQD--NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAP 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2026 PTATSSAPVAVPSTAPVTYPmPQTQMGCSQPPKMEAP-AIRPPSHATAAPhKTPAPVQSSSAsvlNVNHIKRPHSVPSSV 2104
Cdd:pfam03154  228 HTLIQQTPTLHPQRLPSPHP-PLQPMTQPPPPSQVSPqPLPQPSLHGQMP-PMPHSLQTGPS---HMQHPVPPQPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2105 Q--------LPSTLSTQSACQNSVHPANKPVA----PNFSAPLPFGPFStLFENNPTNAHAFWGGPVVSSQSTPeSMLSG 2172
Cdd:pfam03154  303 QssqsqvppGPSPAAPGQSQQRIHTPPSQSQLqsqqPPREQPLPPAPLS-MPHIKPPPTTPIPQLPNPQSHKHP-PHLSG 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2173 KSSYLPNSD--------PLHQSDTSKAPGFRPP----------LQRPAPSPSGIVNMDT--PYGSVTPSSTHLGNFASSL 2232
Cdd:pfam03154  381 PSPFQMNSNlppppalkPLSSLSTHHPPSAHPPplqlmpqsqqLPPPPAQPPVLTQSQSlpPPAASHPPTSGLHQVPSQS 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2233 SGGQM-YGPGAPLGGAPLGGAPTAANfnrqhfsplslltpcSSASNESPAQSVSSGVRAPSPAPSSVPLGS----EKPSS 2307
Cdd:pfam03154  461 PFPQHpFVPGGPPPITPPSGPPTSTS---------------SAMPGIQPPSSASVSSSGPVPAAVSCPLPPvqikEEALD 525
                          410       420
                   ....*....|....*....|....*...
gi 568936357  2308 VSQDRKVPVPigTERSARIRQTGTSAPS 2335
Cdd:pfam03154  526 EAEEPESPPP--PPRSPSPEPTVVNTPS 551
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1617-1678 1.32e-08

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 53.48  E-value: 1.32e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKqKDKTGDrIITIRGGTESTRQATQLINA 1678
Cdd:cd22452     6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESD-VITLRGTKEGVEKAEEMIKK 65
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-618 1.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  233 YVDVVKVLLESGASIeDHNENGHT--------PLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYK----GH 300
Cdd:PHA02878    9 YTDNYETILKYIEYI-DHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEpnklGM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  301 LEMVRFLLEAGADQEHKtdemhtALMEACMDGHVEVARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGASL 380
Cdd:PHA02878   87 KEMIRSINKCSVFYTLV------AIKDAFNNRNVEIFKIIL---------TNRYKN------------------IQTIDL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  381 EEVNDEGYTPLMEAaregheEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcSTPLMEAAQ 460
Cdd:PHA02878  134 VYIDKKSKDDIIEA------EITKLLLSYGADINMKDRHKG------------------------------NTALHYATE 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  461 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL-MKAARAGHVCTVQFLISK 539
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  540 GANVNRTTANNDHTVLSLACAGGHlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLAAPPPDV 618
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
Ank_4 pfam13637
Ankyrin repeats (many copies);
387-441 3.57e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568936357   387 GYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLI 441
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1612-1682 4.82e-08

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 52.41  E-value: 4.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1612 RRSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIKD 1682
Cdd:cd22446     6 KVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEddddetveISIEGDAEGVELAKKEIEAIVKE 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
517-571 5.13e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 5.13e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568936357   517 GRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLL 571
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1076-1178 5.74e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1076 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVV 1155
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 568936357 1156 SLLL-------DRKANVEHRAKTGLTPLME 1178
Cdd:PTZ00322  165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
290-341 7.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 7.66e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357   290 SALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 341
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
201-505 8.08e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 8.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  201 VKIVKLLLAHKADVNAQS--STGNTAL---TYACAGGYVDVVKVLLESGASIEDHNENGHTPLM---EAGSAGHVEVARL 272
Cdd:PHA02989   50 IKIVKLLIDNGADVNYKGyiETPLCAVlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  273 LLENGAGINTHSNE--FKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVArllldsgaqvnmp 350
Cdd:PHA02989  130 LLSKGINVNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVI------------- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  351 adsfespltlaacggHVELAALLIERGASLEEvNDEGYTPLMEAAREGHEEMValllgqganinaqteeTQEtaltlacc 430
Cdd:PHA02989  197 ---------------SIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------------KKE-------- 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  431 ggfLEVADFL---IKAGADIELGCsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQ 505
Cdd:PHA02989  237 ---FKVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1614-1678 1.01e-07

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411949  Cd Length: 76  Bit Score: 51.21  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1678
Cdd:cd22521     6 SHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINA 70
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1617-1681 1.17e-07

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 51.26  E-value: 1.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIK 1681
Cdd:cd22447     8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADedddtmveVTITGDEFNVQHAKQRIEEIIS 80
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1619-1676 1.29e-07

first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the first one.


Pssm-ID: 411828 [Multi-domain]  Cd Length: 68  Bit Score: 50.73  E-value: 1.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTG-DRIITIRGGTESTRQATQLI 1676
Cdd:cd22400     6 VPSEFVGAIIGKGGATIRQITQQTGARIDIHRKENAGAaEKAITIYGTPEGCSSACKQI 64
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1128-1293 1.46e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1128 GSDINAQIETNRNTALTLacfqGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1207
Cdd:PLN03192  518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1208 DTALTIAADKGHYKFCELLIgKGAHIDVRNKKGNTpLWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVK 1287
Cdd:PLN03192  592 NTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                  ....*.
gi 568936357 1288 VVRYLV 1293
Cdd:PLN03192  670 MVRLLI 675
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1616-1681 1.57e-07

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 50.35  E-value: 1.57e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDkqkDKTGDRIITIRGGTESTRQATQLINALIK 1681
Cdd:cd22449     7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE---DKTGEGNVEIKGSKKNVEEAKKRILSQID 69
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1619-1680 1.62e-07

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 50.33  E-value: 1.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22396     7 VPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
PHA02878 PHA02878
ankyrin repeat protein; Provisional
961-1149 1.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  961 DIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSeRTKDTP 1040
Cdd:PHA02878  159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1041 LSLACSggrqevvelllargankehrNVSDYtplslaasggyvNIIKILLNAGAEINSRTgSKLGISPLMLAAMNghTAA 1120
Cdd:PHA02878  238 LHISVG--------------------YCKDY------------DILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERK 282
                         170       180
                  ....*....|....*....|....*....
gi 568936357 1121 VKLLLDMGSDINAqIETNRNTALTLACFQ 1149
Cdd:PHA02878  283 LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
195-274 1.92e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  195 AANGGHVKIvKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 274
Cdd:PTZ00322   90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
681-780 1.93e-07

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   681 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 757
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 568936357   758 -KVERELQLKTQQQLKKQYLEVKA 780
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
Ank_5 pfam13857
Ankyrin repeats (many copies);
989-1044 2.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 2.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   989 LLERG-ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLA 1044
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
1107-1159 2.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568936357  1107 SPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLL 1159
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
681-780 2.49e-07

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 52.92  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  681 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 756
Cdd:COG2825    30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                          90       100
                  ....*....|....*....|....*
gi 568936357  757 -QKVERELQLKTQQQLKKQYLEVKA 780
Cdd:COG2825   103 qQEAQQDLQKRQQELLQPILEKIQK 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
125-308 2.64e-07

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: 56.17  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 198
Cdd:cd22192    21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  199 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 260
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568936357  261 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 308
Cdd:cd22192   180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1614-1677 2.81e-07

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 49.51  E-value: 2.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLIN 1677
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDL--PEENSDSDVITITGKKEDVEKARERIL 62
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
1614-1676 3.30e-07

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 49.73  E-value: 3.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22514     2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsGTRNRKVTITGPQDAVQMAQYLL 67
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1936-2344 3.69e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1936 PAQPGGVSRNSPLDCGSASPNKGASASEQEASSPPVVEPansrPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQV 2015
Cdd:PHA03307   78 EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP----PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2016 PSPDVRMTVPPTATSSAPVAVPStapvtyPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASvlnvnhik 2095
Cdd:PHA03307  154 AAGASPAAVASDAASSRQAALPL------SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS-------- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2096 rphsvPSSVQLPStlstqsacqnsvhPANKPVAPNFSAPLPFGPFSTLFENNPTnahafwGGPVVSSQSTPESMLSGKSS 2175
Cdd:PHA03307  220 -----PAPAPGRS-------------AADDAGASSSDSSSSESSGCGWGPENEC------PLPRPAPITLPTRIWEASGW 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2176 YLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSThlGNFASSLSGGQMYGPGAPLGGAPLGGAPTA 2255
Cdd:PHA03307  276 NGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE--SSSSSTSSSSESSRGAAVSPGPSPSRSPSP 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2256 AnfnrqhfSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSQDRKVPVPIGTERSARIRQTGTS-AP 2334
Cdd:PHA03307  354 S-------RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASgAF 426
                         410
                  ....*....|
gi 568936357 2335 SVIGSNLSTS 2344
Cdd:PHA03307  427 YARYPLLTPS 436
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
966-1145 5.87e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  966 TESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQsERTKDTPLSLAC 1045
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1046 SGGRQEVVELLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLL 1125
Cdd:PLN03192  600 SAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLI 675
                         170       180
                  ....*....|....*....|
gi 568936357 1126 DMGSDINAQIETNRNTALTL 1145
Cdd:PLN03192  676 MNGADVDKANTDDDFSPTEL 695
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1051-1289 6.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 54.75  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1051 EVVELLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAV--- 1121
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1122 KLLLDMGSDINAQIETNRNTAL--TLACFQGRTEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1194
Cdd:PHA02989  128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1195 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADN 1271
Cdd:PHA02989  208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
                         250
                  ....*....|....*...
gi 568936357 1272 RKITPLMAAFRKGHVKVV 1289
Cdd:PHA02989  288 DGDTVLTYAIKHGNIDML 305
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
521-625 6.48e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  521 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 600
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 568936357  601 CYLLDYPN---NLLAAPPPDVTQLTPPS 625
Cdd:PTZ00322  165 QLLSRHSQchfELGANAKPDSFTGKPPS 192
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1618-1677 7.00e-07

fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411827 [Multi-domain]  Cd Length: 67  Bit Score: 48.37  E-value: 7.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1618 SVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKD-KTGDRIITIRGGTESTRQATQLIN 1677
Cdd:cd22399     5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPpNPNEKLFIIRGNPQQIEHAKQLIR 65
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
1614-1678 9.19e-07

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 48.57  E-value: 9.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1678
Cdd:cd22522    10 THELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINA 74
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
956-1192 1.03e-06

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: 54.32  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   956 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1032
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1033 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1098
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1099 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1151
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 568936357  1152 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1192
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1619-1662 1.11e-06

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 47.99  E-value: 1.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITI 1662
Cdd:cd22459     8 CPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITI 51
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1618-1676 1.18e-06

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411916  Cd Length: 69  Bit Score: 48.17  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1618 SVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLI 1676
Cdd:cd22488     5 SIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDpnfKLFIIRGSPQQIDHAKQLI 66
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1107-1294 1.21e-06

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: 53.86  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1107 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1181
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1182 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLwlaan 1249
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1250 ggHLDVVQ-----------LLVQATADVDAA------DNRKITPLMAAFRKGHVKVVRYLVK 1294
Cdd:cd22192   174 --HILVLQpnktfacqmydLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
1071-1125 1.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568936357  1071 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLL 1125
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1616-1676 2.75e-06

first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411863 [Multi-domain]  Cd Length: 73  Bit Score: 47.15  E-value: 2.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22435     5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDfypGTTERVCLIQGEVEAVNAVLDFI 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
696-774 2.87e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTELEQRIKEAIEK----NAQLQSLElAHADQLTKEkIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ-- 769
Cdd:COG4372    76 EQLEEELEELNEQLQAAQAElaqaQEELESLQ-EEAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElk 153

                  ....*
gi 568936357  770 QLKKQ 774
Cdd:COG4372   154 ELEEQ 158
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
1619-1676 2.98e-06

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 46.75  E-value: 2.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22395     6 VPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLI 63
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1617-1680 3.00e-06

third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 46.87  E-value: 3.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22398     4 VPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRICVITGPPDQVQHAARMIQELI 67
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1619-1680 3.76e-06

second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 46.49  E-value: 3.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd02396     8 VPASQCGSLIGKGGSKIKEIRESTGASVQVASEMlPNSTERAVTISGSPEAITKCVEQICCVM 70
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1239-1271 4.53e-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: 45.36  E-value: 4.53e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568936357  1239 KGNTPLWLAA-NGGHLDVVQLLVQATADVDAADN 1271
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
1159-1294 4.57e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1159 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIGKGAHIDV 1235
Cdd:PHA03095    1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1236 RNKKGNTPLWL-AANGGHLDVVQLLVQATADVDAADNRKITPL---MAAFRKgHVKVVRYLVK 1294
Cdd:PHA03095   79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
323-539 4.70e-06

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: 51.94  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  323 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIErgASLEEVND-------EGYTPLMEA 394
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  395 AREGHEEMVALLLGQGANInaqteetqetaLTLACCGGFlevadFLIKAGADIELGcSTPLMEAAQEGHLELVKYLLAAG 474
Cdd:cd22192    97 VVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  475 ANVHATTATGDTAL---------TYACEnghtdVADVLL-----QAGADLEHESEG-GRTPLMKAARAGHVCTVQFLISK 539
Cdd:cd22192   160 ADIRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1018-1200 4.72e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1018 VVEILLDNGadiEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1097
Cdd:PLN03192  509 VGDLLGDNG---GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1098 SRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrntALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLM 1177
Cdd:PLN03192  586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                         170       180
                  ....*....|....*....|...
gi 568936357 1178 EAASGGYAEVGRVLLDKGADVNA 1200
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVDK 683
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1618-1677 5.95e-06

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411917 [Multi-domain]  Cd Length: 69  Bit Score: 46.08  E-value: 5.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1618 SVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLIN 1677
Cdd:cd22489     5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDpnvRIFTIRGVPQQIEHARQLID 67
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1624-1676 6.03e-06

first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 45.71  E-value: 6.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1624 ISRVIGRGGCNINAIRECTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22438    10 VGSIIGKKGETIKKFREESGARINI--SDGSCPERIVTVTGTTDAVFKAFELI 60
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
1619-1676 6.35e-06

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 46.06  E-value: 6.35e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDK---TGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22437     5 VPNSSCGLIIGKGGSTIKELREDSNANIKISPKDQLlpgSSERIVTITGSFDQVVKAVALI 65
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
386-418 6.51e-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: 44.97  E-value: 6.51e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568936357   386 EGYTPLMEAA-REGHEEMVALLLGQGANINAQTE 418
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1120-1321 6.78e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.28  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1120 AVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRA--KTGLTPLM---EAASGGYAEVGRVLLDK 1194
Cdd:PHA02989   18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1195 GADVNAPPVPSSRDTALTIAadKGHYKFCE---LLIGKGAHI-DVRNKKGNTPL--WLAANGGHLDVVQLLVQATADV-D 1267
Cdd:PHA02989   98 GADINLKTFNGVSPIVCFIY--NSNINNCDmlrFLLSKGINVnDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1268 AADNRKITPLMAAFRKG----HVKVVRYLVK-----EVNQFPSDSECMRYIAtiTDKEMLKKC 1321
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKkgvniETNNNGSESVLESFLD--NNKILSKKE 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
1039-1090 7.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.04e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357  1039 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 1090
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1619-1680 7.54e-06

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 45.69  E-value: 7.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1619 VPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDK-----TGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22460     6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEEELppcasPDDRVVQISGEAQAVKKALELVSSRL 72
Ank_4 pfam13637
Ankyrin repeats (many copies);
1005-1057 8.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 8.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568936357  1005 TPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLL 1057
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1105-1261 9.02e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1105 GISPLMLAAMN---GHTAAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRTEVVSLLLDRKANVEHRA-- 1169
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1170 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1225
Cdd:cd21882   106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568936357 1226 LIGKGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1261
Cdd:cd21882   183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1615-1681 9.17e-06

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 45.25  E-value: 9.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDriITIRGGTESTRQATQLINALIK 1681
Cdd:cd02394     4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE--IRIEGSPEGVKKAKAEILELVD 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
1172-1227 9.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 9.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  1172 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1227
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
273-325 9.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568936357   273 LLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 325
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
692-774 9.68e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 9.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEELNKTREEQIQKKQKILEELQK-VERELQLKTQQ 769
Cdd:TIGR04523  359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKLQQEKELLEKeIERLKETIIKN 438
                           90
                   ....*....|
gi 568936357   770 Q-----LKKQ 774
Cdd:TIGR04523  439 NseikdLTNQ 448
PHA02875 PHA02875
ankyrin repeat protein; Provisional
455-606 1.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQ 534
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357  535 FLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDY 606
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1176-1259 1.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1176 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGG 1251
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                  ....*...
gi 568936357 1252 HLDVVQLL 1259
Cdd:PTZ00322  160 FREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
207-258 1.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568936357   207 LLAHK-ADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 258
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03378 PHA03378
EBNA-3B; Provisional
1966-2205 1.04e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.22  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1966 ASSPPVVEPANSRPPHSSSssgsssghsTQQQPPGSVPQEPRPPlQQSQVPSPdvrmtvPPTATSSApVAVPSTAPVTYP 2045
Cdd:PHA03378  683 TMLPIQWAPGTMQPPPRAP---------TPMRPPAAPPGRAQRP-AAATGRAR------PPAAAPGR-ARPPAAAPGRAR 745
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2046 MPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASvlnvnhiKRPHSVPSSVQLPSTLstqsacqnsvhPANK 2125
Cdd:PHA03378  746 PPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQ-------QRPRGAPTPQPPPQAG-----------PTSM 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2126 PVAPNfSAPLPFGPFSTLFENNPTNAHAFwGGPVVSSQSTPESMlsgkSSYLPNSDPlhQSDTS----KAPGFRPPLQRP 2201
Cdd:PHA03378  808 QLMPR-AAPGQQGPTKQILRQLLTGGVKR-GRPSLKKPAALERQ----AAAGPTPSP--GSGTSdkivQAPVFYPPVLQP 879

                  ....
gi 568936357 2202 APSP 2205
Cdd:PHA03378  880 IQVM 883
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
258-362 1.15e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  258 LMEAGSAGHVEVARLLLENGAgiNTHSNEFKESA-LTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 336
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568936357  337 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 362
Cdd:PTZ00322  164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
386-415 1.20e-05

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: 44.12  E-value: 1.20e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568936357    386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1616-1685 1.22e-05

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 45.28  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIdKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDK 1685
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF-PDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-228 1.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568936357   190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYA 228
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
310-408 1.29e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  310 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 380
Cdd:PTZ00322   62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                          90       100
                  ....*....|....*....|....*...
gi 568936357  381 EEVNDEGYTPLMEAAREGHEEMVALLLG 408
Cdd:PTZ00322  142 TLLDKDGKTPLELAEENGFREVVQLLSR 169
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
1621-1682 1.33e-05

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 44.97  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1621 STVISRVIGRGGCNINAIRECTGAHIDIDKQKDktgDRIITIRGGTESTRQATQLINALIKD 1682
Cdd:cd22430     8 SSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQ---EAEVKIFGSDEAQQKAKELIDELVGR 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1009-1113 1.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1009 LAATAGHVGVvEILLDNGADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 1088
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568936357 1089 LL---------NAGAEINSRTG--SKLGISPLMLAA 1113
Cdd:PTZ00322  167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
667-774 1.97e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   667 SKQKSNSHLPANSQDVQGYITN--QSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLElAHADQLTKEKIEELNKTREE 744
Cdd:TIGR04523  236 KKQQEINEKTTEISNTQTQLNQlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKS 314
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568936357   745 QIQKKQKILEELQKverEL--------QLKTQ-QQLKKQ 774
Cdd:TIGR04523  315 ELKNQEKKLEEIQN---QIsqnnkiisQLNEQiSQLKKE 350
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1113-1202 2.26e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1113 AMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1192
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                          90
                  ....*....|....*
gi 568936357 1193 -----DKGADVNAPP 1202
Cdd:PTZ00322  169 rhsqcHFELGANAKP 183
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
691-773 2.33e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  691 PESIVEEAQGKLTELEQRIKEAIEKNAQLQ-SLE--LAHADQLtkekIEELNKTREEQIQKKQKILEELQKVERELQLKT 767
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEELErELEqkAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA 575

                  ....*.
gi 568936357  768 QQQLKK 773
Cdd:PRK00409  576 QQAIKE 581
PHA03247 PHA03247
large tegument protein UL36; Provisional
1742-2110 2.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1742 PAISSASTHKTIKNPVNNVRPGFPVSLPL--AYPPPQFAHALLAAQTFQQIRP-PRLPMTHFGGTFPPA-QSTWGPFPVR 1817
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPePAPHALVSATPLPPGpAAARQASPAL 2735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1818 PLSPA--RATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTASSSASAVPGTTSNGSPSSPSVRRQLFVTVVKTSNA 1895
Cdd:PHA03247 2736 PAAPAppAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1896 TTTTVTTTASNNSTAPTNATypmPTAkehypvsspsspspPAQPGGVSRNSPLDCGSASPNkGASASEQEASSPPVVEPA 1975
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQ---PTA--------------PPPPPGPPPPSLPLGGSVAPG-GDVRRRPPSRSPAAKPAA 2877
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1976 NSRPPHSSSSSGSSsghstqQQPPGSVPQePRPPLQ-------------QSQVPSPDVRMTVPPTATSSAPVAVPSTAPV 2042
Cdd:PHA03247 2878 PARPPVRRLARPAV------SRSTESFAL-PPDQPErppqpqappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPA 2950
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2043 TYPMPQ-----TQMGCSQPPKMEAPAIRPPSHA---------TAAPHKTPAPVQSSSASVLNVnHIKrphSVPSSVQLPS 2108
Cdd:PHA03247 2951 GAGEPSgavpqPWLGALVPGRVAVPRFRVPQPApsreapassTPPLTGHSLSRVSSWASSLAL-HEE---TDPPPVSLKQ 3026

                  ..
gi 568936357 2109 TL 2110
Cdd:PHA03247 3027 TL 3028
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
190-217 2.70e-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: 43.05  E-value: 2.70e-05
                           10        20
                   ....*....|....*....|....*....
gi 568936357   190 TPLMAAA-NGGHVKIVKLLLAHKADVNAQ 217
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
123-376 2.99e-05

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: 49.69  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   123 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 199
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   200 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 277
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   278 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 328
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568936357   329 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 376
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
304-373 3.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 3.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  304 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 373
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
692-768 3.30e-05

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 44.45  E-value: 3.30e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   692 ESIVEEAQgklTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEElnkTREEQIQKKQKILEELQKVERELQLKTQ 768
Cdd:TIGR02926   12 EELIEEAE---EERKQRIAEAREEARELLEEAEEEASKLGEEIIKE---AEEEIEKEAEKIREEGEKEIEAMKSKAK 82
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1958-2317 3.69e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1958 GASASEQEASSPPVVEPANSRPPhsssssgsssghstqQQPPGSVPQEPRPPLQQSQVPSPDVRMTVPPTATSSAPVAVP 2037
Cdd:PRK07764  390 GAGAPAAAAPSAAAAAPAAAPAP---------------AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAP 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2038 STAPVTYP-MPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASVLNVNHIKRphSVPSSVQLPSTLStqsac 2116
Cdd:PRK07764  455 SPPPAAAPsAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRE--RWPEILAAVPKRS----- 527
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2117 qNSVHPAnkpVAPNFSAPLPFGPFSTLFENNPTNAHAF--------------------WGGPVV---SSQSTPESMLSGK 2173
Cdd:PRK07764  528 -RKTWAI---LLPEATVLGVRGDTLVLGFSTGGLARRFaspgnaevlvtalaeelggdWQVEAVvgpAPGAAGGEGPPAP 603
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2174 SSYLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHLGNFASSLSGGQMYGPGAPLGGAPLGGAP 2253
Cdd:PRK07764  604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP 683
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357 2254 TAANFNRQHFSPlsllTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSqDRKVPVP 2317
Cdd:PRK07764  684 APAPAAPAAPAG----AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA-DDPVPLP 742
Ank_5 pfam13857
Ankyrin repeats (many copies);
446-491 3.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.94e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568936357   446 DIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYA 491
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1628-1676 4.78e-05

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 43.40  E-value: 4.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357 1628 IGRGGCNINAIRECTGAHIDIDKQKDKTGDrIITIRGGTESTRQATQLI 1676
Cdd:cd22413    18 IGRGGANIRKIRDNTGARIIFPTARDEDQE-LITIIGTKEAVEKAKEEL 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1105-1133 4.85e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 4.85e-05
                           10        20
                   ....*....|....*....|....*....
gi 568936357  1105 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1133
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
228-381 5.18e-05

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: 48.54  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   228 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 302
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   303 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 357
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 568936357   358 LTLAACGGHVELAALLIERGASLE 381
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
1139-1192 5.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568936357  1139 RNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1192
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
213-407 5.58e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.34  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  213 DVNAQSSTGNTALTYAC---AGGYVDVVKVLLESG-----------ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGA 278
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  279 GINTHSN------------EFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSG 344
Cdd:cd21882    98 DVSARATgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENS 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357  345 AQVnmpADSFESPLTLAACGGHVElaalliergaSLEEV-NDEGYTPLMEAAREGHEEMVALLL 407
Cdd:cd21882   174 AFV---CQMYNLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02859 PHA02859
ankyrin repeat protein; Provisional
201-315 5.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  201 VKIVKLLLAHKADVNAQSSTGNTAL--TYACAGGYV--DVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLL 273
Cdd:PHA02859   66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568936357  274 LENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQE 315
Cdd:PHA02859  145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1002-1032 6.34e-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: 41.89  E-value: 6.34e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568936357  1002 KGFTPLILAAT-AGHVGVVEILLDNGADIEAQ 1032
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
452-538 6.38e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  452 STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVC 531
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*..
gi 568936357  532 TVQFLIS 538
Cdd:PTZ00322  163 VVQLLSR 169
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1938-2139 6.44e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1938 QPGGVSRNSPLDCGSASPnkgASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPS 2017
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAP---VAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2018 PDVRMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASVLNVNHIKRP 2097
Cdd:PRK12323  441 ARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568936357 2098 HSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGP 2139
Cdd:PRK12323  521 WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
453-481 7.07e-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: 41.89  E-value: 7.07e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357   453 TPLMEAA-QEGHLELVKYLLAAGANVHATT 481
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
517-547 7.21e-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: 41.89  E-value: 7.21e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568936357   517 GRTPLMKAA-RAGHVCTVQFLISKGANVNRTT 547
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
681-773 7.65e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.88  E-value: 7.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357    681 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 756
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 568936357    757 QKV-ERELQLKTQQQLKK 773
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
PTZ00121 PTZ00121
MAEBL; Provisional
696-779 7.72e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTEL--EQRIKEAIEKNAQLQSLELAHADQLTKEkiEELNKTREEQIQKK----QKILEELQKVERElQLKTQQ 769
Cdd:PTZ00121 1616 EEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKaeedKKKAEEAKKAEED-EKKAAE 1692
                          90
                  ....*....|
gi 568936357  770 QLKKQYLEVK 779
Cdd:PTZ00121 1693 ALKKEAEEAK 1702
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1105-1133 7.76e-05

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: 41.80  E-value: 7.76e-05
                            10        20
                    ....*....|....*....|....*....
gi 568936357   1105 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1133
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
695-780 8.05e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKL----TELEQRIKEAIEKNAQLQSL--ELAHADQLTKEKIEELNKTREEQIQKKQKIlEELQKvERELQLKTQ 768
Cdd:COG4372    54 LEQAREELeqleEELEQARSELEQLEEELEELneQLQAAQAELAQAQEELESLQEEAEELQEEL-EELQK-ERQDLEQQR 131
                          90
                  ....*....|..
gi 568936357  769 QQLKKQYLEVKA 780
Cdd:COG4372   132 KQLEAQIAELQS 143
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
1616-1680 8.25e-05

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 42.69  E-value: 8.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22454     7 EVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
PHA02798 PHA02798
ankyrin-like protein; Provisional
1018-1249 9.38e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1018 VVEILLDNGADIEAQsERTKDTPLSLACSGGRQ-----EVVELLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 1089
Cdd:PHA02798   53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1090 LNAGAEINSRtgSKLGISPLMLAAMNGHTA---AVKLLLDMGSDINaqIETNRNTALTLACFQGRT------EVVSLLLD 1160
Cdd:PHA02798  132 IENGADTTLL--DKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDIN--THNNKEKYDTLHCYFKYNidridaDILKLFVD 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1161 -----RKANVEHRAKtgLTPLMEAASGGYAEVGRVLLD---KGADVNAPPVPSSrdTALTIAADKGHYKFCELLIGKGAH 1232
Cdd:PHA02798  208 ngfiiNKENKSHKKK--FMEYLNSLLYDNKRFKKNILDfifSYIDINQVDELGF--NPLYYSVSHNNRKIFEYLLQLGGD 283
                         250
                  ....*....|....*..
gi 568936357 1233 IDVRNKKGNTPLWLAAN 1249
Cdd:PHA02798  284 INIITELGNTCLFTAFE 300
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1614-1682 1.03e-04

fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 42.57  E-value: 1.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIR-ECTGAHIDIDKQKDKtgdriITIRGGTESTRQATQLINALIKD 1682
Cdd:cd22409     3 VAEVSAPSWLHRFIIGKKGANIKKITqDLPKVHIEFTEGEDK-----IELEGPPEEVEVVREQLEAIVKE 67
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
386-415 1.12e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 1.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357   386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1614-1680 1.17e-04

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 42.24  E-value: 1.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22479     2 TEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKMMLDDIV 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1949-2086 1.25e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1949 DCGSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQ-QPPGSVPQEPRPPLQQSQVPSPDVRMTVPPT 2027
Cdd:PRK07764  585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAaAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 2028 ATSSAPVAVPSTAPVTYPMPQtqmgcsQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSA 2086
Cdd:PRK07764  665 GGDGWPAKAGGAAPAAPPPAP------APAAPAAPAGAAPAQPAPAPAATPPAGQADDP 717
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1002-1031 1.39e-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: 41.03  E-value: 1.39e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568936357   1002 KGFTPLILAATAGHVGVVEILLDNGADIEA 1031
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
453-479 1.44e-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: 41.03  E-value: 1.44e-04
                            10        20
                    ....*....|....*....|....*..
gi 568936357    453 TPLMEAAQEGHLELVKYLLAAGANVHA 479
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
253-281 1.48e-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: 41.12  E-value: 1.48e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357   253 NGHTPLMEA-GSAGHVEVARLLLENGAGIN 281
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1911-2303 1.49e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1911 PTNATYPMPTAkehyPVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKGASASEQEASSP--PVVEP---ANSRPPHSSSS 1985
Cdd:pfam05109  455 PTNLTAPASTG----PTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPtsAVTTPtpnATSPTPAVTTP 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1986 SGSSSGHSTQQQPPGSVPQEPRP----PLQQSQVPSPDVrmTVP-------------PTATSSAPvAVPSTAPVTYPMPQ 2048
Cdd:pfam05109  531 TPNATSPTLGKTSPTSAVTTPTPnatsPTPAVTTPTPNA--TIPtlgktsptsavttPTPNATSP-TVGETSPQANTTNH 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2049 TQMGCSQPPKMEApairPPSHATAAPHKTPAPVQSSSASVLNVnhikRPHSVPSSVQlPSTLSTQSACQNSVHPANKPVA 2128
Cdd:pfam05109  608 TLGGTSSTPVVTS----PPKNATSAVTTGQHNITSSSTSSMSL----RPSSISETLS-PSTSDNSTSHMPLLTSAHPTGG 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2129 PNFSAPLPfgpfstlfenNPTNAHAfwggpVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAP-SPSG 2207
Cdd:pfam05109  679 ENITQVTP----------ASTSTHH-----VSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPqAPSG 743
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2208 ivnmdtpYGSVTPSSTHLGNFASSLSGGQ-MYGPGAPLGGAPLGGAPTAANFNRQHFSPLSLLTPcSSASNESPAQSVSS 2286
Cdd:pfam05109  744 -------QKTAVPTVTSTGGKANSTTGGKhTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPP-STSSKLRPRWTFTS 815
                          410
                   ....*....|....*..
gi 568936357  2287 GVRAPSPAPSSVPLGSE 2303
Cdd:pfam05109  816 PPVTTAQATVPVPPTSQ 832
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
517-544 1.62e-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: 40.65  E-value: 1.62e-04
                            10        20
                    ....*....|....*....|....*...
gi 568936357    517 GRTPLMKAARAGHVCTVQFLISKGANVN 544
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1225-1292 1.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1225 LLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYL 1292
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
235-409 1.77e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  235 DVVKVLLEsgASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGIN----------THSNE---FKESALTLACYKGHL 301
Cdd:cd22194   124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  302 EMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaSLE 381
Cdd:cd22194   202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
                         170       180
                  ....*....|....*....|....*....
gi 568936357  382 EV-NDEGYTPLMEAAREGHEEMVALLLGQ 409
Cdd:cd22194   261 TIrNNEGLTPLQLAAKMGKAEILKYILSR 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
484-511 1.91e-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: 40.65  E-value: 1.91e-04
                            10        20
                    ....*....|....*....|....*...
gi 568936357    484 GDTALTYACENGHTDVADVLLQAGADLE 511
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1239-1268 1.93e-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: 40.65  E-value: 1.93e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568936357   1239 KGNTPLWLAANGGHLDVVQLLVQATADVDA 1268
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
221-249 1.93e-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: 40.65  E-value: 1.93e-04
                            10        20
                    ....*....|....*....|....*....
gi 568936357    221 GNTALTYACAGGYVDVVKVLLESGASIED 249
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
2013-2316 2.02e-04

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 46.96  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2013 SQVPSPDVRMTVPPTATSSAPvavPSTAPVTYPMPQTQMGCSQP--PKMEAPAIRPPSHATAAPHKTP------------ 2078
Cdd:COG5665   253 EEKSSQQPKSQPTSPSGGTTP---PSTNQLTTSNTPTSTAKAQPqpPTKKQPAKEPPSDTASGNPSAPsvlinsdsptse 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2079 APVQSSSASVLNVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGPFSTLFE----NNPTNAHAF 2154
Cdd:COG5665   330 DPATASVPTTEETTAFTTPSSVPSTPAEKDTPATDLATPVSPTPPETSVDKKVSPDSATSSTKSEKEggtaSSPMPPNIA 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2155 WGgpvVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPL-----QRPAPSPSGIVNMDTPYGSVTPSSTHLGNFA 2229
Cdd:COG5665   410 IG---AKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSVRTEAspsagSDLEPENTTLRDPAPNAIPPPEDPSTIGRLS 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2230 SSLSGGQMYGPGAPLGGAPLGGAPTAANFNRQHFSPlslltpcssASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVS 2309
Cdd:COG5665   487 SGDKLANETGPPVIRRDSTPSSTADQSIVGVLAFGL---------DQRTQAEISVEAASRSNPLLNSQVKSFPLGKRSEG 557

                  ....*..
gi 568936357 2310 QDRKVPV 2316
Cdd:COG5665   558 AKGKTQT 564
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
1615-1676 2.11e-04

type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic recombination 1 protein (MER1) and similar proteins; MER1 is required for chromosome pairing and genetic recombination. It may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 41.67  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 1615 KKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTgDRIITIRGGTESTRQATQLI 1676
Cdd:cd22458     3 WEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNSS-QQTIHLSGTDKQIALAISSI 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
373-428 2.11e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   373 LIERG-ASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETqETALTLA 428
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1617-1672 2.36e-04

fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 41.46  E-value: 2.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDI--DKQKDKTGDRIITIRGGTESTRQA 1672
Cdd:cd22403     4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLprDQTPDEGDEVPVEIIGNFYATQSA 61
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
962-1091 2.47e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.29  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  962 IDAQ-TESNHD--TALTLACAGGHEELVQTLLERGASIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 1024
Cdd:cd22194   130 INAEyTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1025 NGADIEAQSERTKDTPL---------SLACSGGRQEVVELLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 1091
Cdd:cd22194   210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
121-341 2.59e-04

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: 46.61  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   121 DNRSLAEACSEGDVNAVRKLLIEgrsVNEHTEEGESLLcLACSAGYY----ELAQVLLAMH--------ANVEDRG-IKG 187
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLN---LSCRGAVGDTLL-HAISLEYVdaveAILLHLLAAFrksgplelANDQYTSeFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   188 DITPLMAAANGGHVKIVKLLLAHKADVNA-------QSSTGNTAL--------TYACAGGYvDVVKVLLESGASIEDHNE 252
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFyhgesplnAAACLGSP-SIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   253 NGHTplmeagsaghveVARLLLENgaginthsNEFKESALTLACykghlEMVRFLLEAGaDQEHKTDEMH--------TA 324
Cdd:TIGR00870  207 LGNT------------LLHLLVME--------NEFKAEYEELSC-----QMYNFALSLL-DKLRDSKELEvilnhqglTP 260
                          250
                   ....*....|....*..
gi 568936357   325 LMEACMDGHVEVARLLL 341
Cdd:TIGR00870  261 LKLAAKEGRIVLFRLKL 277
PHA03379 PHA03379
EBNA-3A; Provisional
1952-2294 2.61e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.59  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1952 SASPNKGASASEQEASS-----------PPVV---EPANSRPPH----------SSSSSGSSSGHSTQQQPPGSVPQEPR 2007
Cdd:PHA03379  338 EGEHDEGATGETREESEdtesdgddeelPRIVsreGTKRKRPPIflrrlhrlllMRAGKLTERAREALEKASEPTYGTPR 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2008 PPLqqsQVPSPDVRMTVpPTATSSAPVAVPSTAPVTYPMPQ-TQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSA 2086
Cdd:PHA03379  418 PPV---EKPRPEVPQSL-ETATSHGSAQVPEPPPVHDLEPGpLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDGRP 493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2087 SVLNV----NHIKRPHSvPSSVQLPSTLSTqsacqnSVHPANKPVAPNfsaPLPFGPFSTlfENNPTNAHAFWGGPVVSS 2162
Cdd:PHA03379  494 ACAPVpapaGPIVRPWE-ASLSQVPGVAFA------PVMPQPMPVEPV---PVPTVALER--PVCPAPPLIAMQGPGETS 561
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2163 QSTPESMLSGKSSYLPNSDplhQSDTSKAPGFRPPLQRPAPSP-SGIVNMDTPYGSVTPSSTHLgnfASSLSGGQMYGPG 2241
Cdd:PHA03379  562 GIVRVRERWRPAPWTPNPP---RSPSQMSVRDRLARLRAEAQPyQASVEVQPPQLTQVSPQQPM---EYPLEPEQQMFPG 635
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568936357 2242 APLGG-APLGGAPTAANFNRQHFSpLSLLTPCSSASNESPAQSvSSGVRAPSPA 2294
Cdd:PHA03379  636 SPFSQvADVMRAGGVPAMQPQYFD-LPLQQPISQGAPLAPLRA-SMGPVPPVPA 687
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
1963-2067 2.65e-04

VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion];


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 44.95  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1963 EQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVPPTATSSAPVAVPSTAPV 2042
Cdd:COG5066   121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                          90       100
                  ....*....|....*....|....*
gi 568936357 2043 TYPMPQTQMGCSQPPKMEAPAIRPP 2067
Cdd:COG5066   201 STPKPQNQIKEAATVPAENEPSSMP 225
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1617-1680 2.70e-04

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3.


Pssm-ID: 411891 [Multi-domain]  Cd Length: 71  Bit Score: 41.26  E-value: 2.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22463     6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYplEETQKILRISGTEEQLKRAQSLVEGLI 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
190-216 2.73e-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: 40.26  E-value: 2.73e-04
                            10        20
                    ....*....|....*....|....*..
gi 568936357    190 TPLMAAANGGHVKIVKLLLAHKADVNA 216
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
158-251 2.75e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  158 LCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 237
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90
                  ....*....|....
gi 568936357  238 KVLleSGASIEDHN 251
Cdd:PTZ00322  165 QLL--SRHSQCHFE 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1105-1134 2.85e-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: 39.97  E-value: 2.85e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568936357  1105 GISPLMLAA-MNGHTAAVKLLLDMGSDINAQ 1134
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
667-779 2.90e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   667 SKQKSNSHLPANSQDVQGYI-----TNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSL--ELAHADQLTKEKIEELN 739
Cdd:TIGR04523  381 SYKQEIKNLESQINDLESKIqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikDLTNQDSVKELIIKNLD 460
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 568936357   740 KTREEQIQKKQKILEELQKVERELQlKTQQQLKKQYLEVK 779
Cdd:TIGR04523  461 NTRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELK 499
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
695-780 3.21e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIE----KNAQLQSLELAHADQltKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQ 770
Cdd:COG1579    98 IESLKRRISDLEDEILELMErieeLEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
                          90
                  ....*....|
gi 568936357  771 LKKQYLEVKA 780
Cdd:COG1579   176 LLALYERIRK 185
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
2007-2159 3.33e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 45.86  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2007 RPPLQQSQVPSPDVRMTVPPTATSSAPVAVPSTAPVTYPMPqtqmgcsQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSA 2086
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAA-------APAAAASAPAAPPAAAPPAPVAAPAAAAPAAA 437
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 2087 svlnvnhikrPHSVPSSVQLPSTLSTQSACQNSVHPAN------KPVAPNFSAPLPFGPFSTlfennPTNAHAFWGGPV 2159
Cdd:PRK14951  438 ----------PAAAPAAVALAPAPPAQAAPETVAIPVRvapepaVASAAPAPAAAPAAARLT-----PTEEGDVWHATV 501
PHA03100 PHA03100
ankyrin repeat protein; Provisional
960-1031 3.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 3.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357  960 IDIDAQTEsNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1031
Cdd:PHA03100  183 VPINIKDV-YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1951-2084 3.60e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 45.86  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1951 GSASPNKGASASEQEASsPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPgSVPQEPRPPlqqSQVPSPDVRMTVPPTATS 2030
Cdd:PRK14951  367 AAAAEAAAPAEKKTPAR-PEAAAPAAAPVAQAAAAPAPAAAPAAAASAP-AAPPAAAPP---APVAAPAAAAPAAAPAAA 441
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568936357 2031 SAPVAVPSTAPvtypmPQTQMGCSQPPKMEAPairPPSHATAAPHKTPAPVQSS 2084
Cdd:PRK14951  442 PAAVALAPAPP-----AQAAPETVAIPVRVAP---EPAVASAAPAPAAAPAAAR 487
PHA02876 PHA02876
ankyrin repeat protein; Provisional
457-556 3.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  457 EAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 536
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                          90       100
                  ....*....|....*....|
gi 568936357  537 ISKGANVNRttanNDHTVLS 556
Cdd:PHA02876  231 IDNRSNINK----NDLSLLK 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
1022-1077 3.70e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  1022 LLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLA 1077
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
709-774 3.85e-04

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


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 40.71  E-value: 3.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  709 IKEaiEKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 774
Cdd:cd22249     7 IRE--EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
2065-2344 4.00e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2065 RPPSHATAAPHK---TPAPVQSSSASVLNVNHIKRPHS---VPSSVQLPStlstqsacqnsvhpankpvapNFSAPLPFG 2138
Cdd:pfam05109  407 RTATNATTTTHKvifSKAPESTTTSPTLNTTGFAAPNTttgLPSSTHVPT---------------------NLTAPASTG 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2139 P-FSTLFENNPTnahafwggpvvssqstPESMLSGKSSYLPNSDPLHQSDTSKAPGFrpplqrpaPSPSGIVNMDTPYG- 2216
Cdd:pfam05109  466 PtVSTADVTSPT----------------PAGTTSGASPVTPSPSPRDNGTESKAPDM--------TSPTSAVTTPTPNAt 521
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2217 SVTPSSTHLGNFASSLSGGQMYGPGAPLGGAPLGGAPTAAnfnrqhfsplsLLTPCSSASNESPAQ-SVSSGVRAPSPAP 2295
Cdd:pfam05109  522 SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPA-----------VTTPTPNATIPTLGKtSPTSAVTTPTPNA 590
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568936357  2296 SSVPLGSEKPSSVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTS 2344
Cdd:pfam05109  591 TSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSS 639
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1613-1689 4.22e-04

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 45.77  E-value: 4.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1689
Cdd:COG1185   549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
PRK12704 PRK12704
phosphodiesterase; Provisional
696-771 4.26e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTELEQRIKEaieKNAQLQSLE---LAHADQLtKEKIEELNK------TREEQIQKKQKILEELQKVERELQLK 766
Cdd:PRK12704   64 EEIHKLRNEFEKELRE---RRNELQKLEkrlLQKEENL-DRKLELLEKreeeleKKEKELEQKQQELEKKEEELEELIEE 139

                  ....*
gi 568936357  767 TQQQL 771
Cdd:PRK12704  140 QLQEL 144
PHA02946 PHA02946
ankyin-like protein; Provisional
980-1176 4.37e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  980 GGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLaCSGGRQEVVE---LL 1056
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYY-LSGTDDEVIErinLL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1057 LARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEinSRTGSKLGISPL--MLAAMNGHTAAVKLLLDMGSDiNAQ 1134
Cdd:PHA02946  127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGIS-PSK 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568936357 1135 IETNRNTALTLACFQ--GRTEVVSLLLDrKANVEHRAKTGLTPL 1176
Cdd:PHA02946  204 PDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
HAUS4 pfam14735
HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. ...
644-779 4.44e-04

HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464287  Cd Length: 235  Bit Score: 44.17  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   644 PPQEPDKP------PANLAATLPVRSKAASKQKS-----NSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEA 712
Cdd:pfam14735    5 PTVGGDQPrllgltPADLLQLMPDKQDVQQMQQRlprelEARLKKKCFALLSYYQPESEGDSEGLKAAKLSRLPELLESE 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   713 IEknaQLQSLELAHADQLTKekieeLNKTREEQIQKKQKILEELQKVERELQLKTQQQL---KKQYLEVK 779
Cdd:pfam14735   85 KR---RLESEKEKLRENLVL-----LQRQFAEYYQVLLQCLQLLQRLVLDHRLKHQSDLdrkKKEYLEAK 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
1089-1146 4.55e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  1089 LLNAGAeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLA 1146
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
PHA03378 PHA03378
EBNA-3B; Provisional
1957-2317 4.59e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1957 KGASASEQEASSP--PVVEPANSRPPhsssssgsssghsTQQQP----PGSVPQ--EPRPPLQQSQVPSpdVRMTVPPTA 2028
Cdd:PHA03378  433 KKAARTEQPRATPhsQAPTVVLHRPP-------------TQPLEgptgPLSVQAplEPWQPLPHPQVTP--VILHQPPAQ 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2029 TSSAPVAVPS-------------TAPVTYPMPQTQMGCSQPP---------KMEAPAIRPPSHATAAPHKTPAPVQ---- 2082
Cdd:PHA03378  498 GVQAHGSMLDllekddedmeqrvMATLLPPSPPQPRAGRRAPcvytedldiESDEPASTEPVHDQLLPAPGLGPLQiqpl 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2083 ----SSSASVLNVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPAN--KPVAPNFSAPLPFGPFSTlfeNNPTNAHAFWG 2156
Cdd:PHA03378  578 tsptTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQwpMPLRPIPMRPLRMQPITF---NVLVFPTPHQP 654
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2157 GPVVSSQSTPESMLSGKSSYLPN-SDPLHQSDTSKAPG-FRPPLQRPAPSP---SGIVNMDTPYGSVTPSSTHLGnfass 2231
Cdd:PHA03378  655 PQVEITPYKPTWTQIGHIPYQPSpTGANTMLPIQWAPGtMQPPPRAPTPMRppaAPPGRAQRPAAATGRARPPAA----- 729
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2232 lSGGQMYGP-GAPLGGAPLGGAPTAANfnrqhfsplslltPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPssvsq 2310
Cdd:PHA03378  730 -APGRARPPaAAPGRARPPAAAPGRAR-------------PPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP----- 790

                  ....*..
gi 568936357 2311 dRKVPVP 2317
Cdd:PHA03378  791 -RGAPTP 796
PHA02884 PHA02884
ankyrin repeat protein; Provisional
233-330 4.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  233 YVDVVKVLLESGASIE---DHNENGHT-PLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLL 308
Cdd:PHA02884   45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 568936357  309 EAGADQEHKTDEMHTALMEACM 330
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
517-544 5.02e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 5.02e-04
                           10        20
                   ....*....|....*....|....*...
gi 568936357   517 GRTPLMKAARAGHVCTVQFLISKGANVN 544
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1613-1689 5.21e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.43  E-value: 5.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357 1613 RSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1689
Cdd:PRK11824  554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-471 5.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 5.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357   423 TALTLACCGGFLEVADFLIKAGADI---ELGCSTPLMEAAQEGHLELVKYLL 471
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADInavDGNGETALHFAASNGNVEVLKLLL 54
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
688-780 5.77e-04

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 43.60  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   688 NQSPESIVEEAQGKLTELEQRIKE---AIEKNAQLQSlelahadQLTKE--KIEELNKTREEQIQKKQKILEELQKVERE 762
Cdd:pfam14988   28 VQECEEIERRRQELASRYTQQTAElqtQLLQKEKEQA-------SLKKElqALRPFAKLKESQEREIQDLEEEKEKVRAE 100
                           90
                   ....*....|....*...
gi 568936357   763 LQLKTQQqLKKQYLEVKA 780
Cdd:pfam14988  101 TAEKDRE-AHLQFLKEKA 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
695-780 5.79e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   695 VEEAQGKLTELEQRIKEaIEKNAQLQSLELAHADQltkeKIEELNKTREEQIQKKQKILEELQKVEREL-QLKTQQQLKK 773
Cdd:TIGR02168  283 IEELQKELYALANEISR-LEQQKQILRERLANLER----QLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLE 357

                   ....*..
gi 568936357   774 QYLEVKA 780
Cdd:TIGR02168  358 AELEELE 364
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
695-780 5.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIEKNAQLQSLELahadqlTKEKIEELNKTREEQIQKKQKILEELQKVERElqLKTQQQLKKQ 774
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEG------SKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEE 294

                  ....*.
gi 568936357  775 YLEVKA 780
Cdd:PRK03918  295 YIKLSE 300
PHA03100 PHA03100
ankyrin repeat protein; Provisional
498-610 5.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  498 DVADVLLQAGADLEHESEGGRTPLMKAARAGHVCT-----VQFLISKGANVNRTTANNDHTVLSLACAG-GHLAVVELLL 571
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568936357  572 AHGADPTHRLKDGSTMLIEAAKGGH--TSVVCYLLDYPNNL 610
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
702-770 6.08e-04

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 40.73  E-value: 6.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  702 LTELEQRIKEAIEKNAQLQslelahadqLTKEKIEELNKTREEQIQKKQKILEELQKVERelQLKTQQQ 770
Cdd:COG3074     6 LEELEAKVQQAVDTIELLQ---------MEVEELKEKNEELEQENEELQSENEELQSENE--QLKTENA 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
322-349 8.11e-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: 8.11e-04
                            10        20
                    ....*....|....*....|....*...
gi 568936357    322 HTALMEACMDGHVEVARLLLDSGAQVNM 349
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1186-1339 8.23e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1186 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATAD 1265
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1266 VDAADNRKITPLMAAFRKGHVKVVRYLvkevNQFPSDS------ECMRYIATITDKEMLKKChLCMESIVQAKDRQAAEA 1339
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRIL----YHFASISdphaagDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATA 658
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
253-281 8.69e-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: 8.69e-04
                            10        20
                    ....*....|....*....|....*....
gi 568936357    253 NGHTPLMEAGSAGHVEVARLLLENGAGIN 281
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
965-1162 9.27e-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: 44.62  E-value: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  965 QTESNHDTALTLACAGGHEELVQTLL--------ERGASiehrdkkGFTPLILAATAGHVGVVEILLDNGADI---EAQS 1033
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGAL-------GETALHVAALYDNLEAAVVLMEAAPELvnePMTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1034 ERTK-DTPLSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEIns 1098
Cdd:cd22192    85 DLYQgETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADI-- 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1099 RTGSKLGISPLMLAAMNGHTAAVKLLLDM-----GSDINAQIETNRN----TALTLACFQGRTEVVSLLLDRK 1162
Cdd:cd22192   163 RAQDSLGNTVLHILVLQPNKTFACQMYDLilsydKEDDLQPLDLVPNnqglTPFKLAAKEGNIVMFQHLVQKR 235
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1029-1257 9.36e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1029 IEAQSERTKDTPLSL--ACSGGRQEVVELLlargANKEHRN-------VSDYTPLSLAASG-GYVNIIKILLNagaeINS 1098
Cdd:cd22194    36 AELAKEEQRDKKKRLkkVSEAAVEELGELL----KELKDLSrrrrktdVPDFLMHKLTASDtGKTCLMKALLN----INE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1099 RTGSklgISPLMLAAMNGHTAAVKLlldmgsdINAQIeTNRN----TALTLACFQGRTEVVSLLLDRKANVEHRAKT--- 1171
Cdd:cd22194   108 NTKE---IVRILLAFAEENGILDRF-------INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvff 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1172 -----------GLTPLMEAASGGYAEVGRVLLDKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------L 1225
Cdd:cd22194   177 npkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiL 251
                         250       260       270
                  ....*....|....*....|....*....|...
gi 568936357 1226 LIGKGAHID-VRNKKGNTPLWLAANGGHLDVVQ 1257
Cdd:cd22194   252 LKSENKNLEtIRNNEGLTPLQLAAKMGKAEILK 284
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
695-780 9.58e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIkEAIEKNAQLQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKV-----ERELQLKTQQ 769
Cdd:COG1196   283 LEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeaeeELEEAEAELA 361
                          90
                  ....*....|.
gi 568936357  770 QLKKQYLEVKA 780
Cdd:COG1196   362 EAEEALLEAEA 372
PRK12704 PRK12704
phosphodiesterase; Provisional
692-777 9.58e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQ------GKLTELE-----QRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKtREEQIQKKQKILE------ 754
Cdd:PRK12704   41 KRILEEAKkeaeaiKKEALLEakeeiHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-KLELLEKREEELEkkekel 119
                          90       100
                  ....*....|....*....|....*...
gi 568936357  755 -----ELQKVERELQLKTQQQLKKqyLE 777
Cdd:PRK12704  120 eqkqqELEKKEEELEELIEEQLQE--LE 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
962-1000 9.95e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 9.95e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568936357   962 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1000
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
692-773 1.03e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIE---ELNKtREEQIQKKQKILEELQKVERELQLKTq 768
Cdd:COG2433   419 EEQVERLEAEVEELEAELEEKDERIERLER-ELSEARSEERREIRkdrEISR-LDREIERLERELEEERERIEELKRKL- 495

                  ....*
gi 568936357  769 QQLKK 773
Cdd:COG2433   496 ERLKE 500
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
698-780 1.14e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 44.29  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   698 AQGKLTELEQRIKEaIEKNAQLQSlelAHADQ--LTKEKIEE-LNKTRE--EQIQKKQKILEELQ-KVERELQLKT---Q 768
Cdd:pfam05622  330 ANQRILELQQQVEE-LQKALQEQG---SKAEDssLLKQKLEEhLEKLHEaqSELQKKKEQIEELEpKQDSNLAQKIdelQ 405
                           90
                   ....*....|..
gi 568936357   769 QQLKKQYLEVKA 780
Cdd:pfam05622  406 EALRKKDEDMKA 417
Ank_5 pfam13857
Ankyrin repeats (many copies);
1157-1214 1.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  1157 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1214
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1997-2108 1.19e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1997 QPPGSVPQEPRPPLQQSQVPspdvRMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHK 2076
Cdd:PRK10263  762 QQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 837
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568936357 2077 TPAPVQSSSASVLNVNHIKRPHSVPSSvQLPS 2108
Cdd:PRK10263  838 APQPQDTLLHPLLMRNGDSRPLHKPTT-PLPS 868
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
969-997 1.24e-03

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: 38.34  E-value: 1.24e-03
                            10        20
                    ....*....|....*....|....*....
gi 568936357    969 NHDTALTLACAGGHEELVQTLLERGASIE 997
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_Rnc1_rpt1 cd22455
first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1627-1676 1.25e-03

first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411883  Cd Length: 70  Bit Score: 39.59  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936357 1627 VIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22455    15 IIGKGGENIARLRATTGVKAGVSKVVPGVHDRVLTVSGPLEGVAKAFGLI 64
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
695-777 1.26e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIEKNAQLQslelAHADQLtKEKIEELNKTREEQIQKKQKILEELQKVERELQL--KTQQQLK 772
Cdd:COG4372   103 LESLQEEAEELQEELEELQKERQDLE----QQRKQL-EAQIAELQSEIAEREEELKELEEQLESLQEELAAleQELQALS 177

                  ....*
gi 568936357  773 KQYLE 777
Cdd:COG4372   178 EAEAE 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
695-774 1.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIEKNAQLQS--LELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQLK 772
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                  ..
gi 568936357  773 KQ 774
Cdd:COG1196   377 AE 378
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1070-1097 1.41e-03

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: 37.95  E-value: 1.41e-03
                            10        20
                    ....*....|....*....|....*...
gi 568936357   1070 DYTPLSLAASGGYVNIIKILLNAGAEIN 1097
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
402-542 1.43e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  402 MVALLlgqgaNINAQTEETQETALTLACCGGFLEVadfLIKAGADIE-LGCSTPLMEAAQEGHLELVKYLLAAGANVHAt 480
Cdd:cd22194    99 MKALL-----NINENTKEIVRILLAFAEENGILDR---FINAEYTEEaYEGQTALNIAIERRQGDIVKLLIAKGADVNA- 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  481 TATGdtaltyacenghtdvadVLLQAgadlEHESEG---GRTPLMKAAraghvCT-----VQFLISKGAN 542
Cdd:cd22194   170 HAKG-----------------VFFNP----KYKHEGfyfGETPLALAA-----CTnqpeiVQLLMEKEST 213
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
974-1162 1.45e-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: 43.92  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   974 LTLACAGGHEELVQTLLERGASIEHRDKkgftpLILAATAGHVGVVE----ILLDNGADI--------EAQSERTKD-TP 1040
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1041 LSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1106
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936357  1107 SPLMLAAMNGHTAAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRTEVVSLLLDRK 1162
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
696-778 1.46e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK--EKI----EELNKTrEEQIQKKQKILEELQKVERELQlKTQQ 769
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAleRRIaalaRRIRAL-EQELAALEAELAELEKEIAELR-AELE 100

                  ....*....
gi 568936357  770 QLKKQYLEV 778
Cdd:COG4942   101 AQKEELAEL 109
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
252-471 1.54e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  252 ENGHTPLMEAgsaghvevarlLLEngagINTHSNEFKESALTLACYKGHLEmvRFLleaGADQEHKTDEMHTALMEACMD 331
Cdd:cd22194    92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  332 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGAsleevndegyTPLMEAARE 397
Cdd:cd22194   152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKES----------TDITSQDSR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  398 GHEEMVALLlgqganINAQTEETQETALTlaccggflEVADFLIKAGADIELGCS------TPLMEAAQEGHLELVKYLL 471
Cdd:cd22194   222 GNTVLHALV------TVAEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYIL 287
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
692-774 1.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQS--LELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ 769
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                  ....*
gi 568936357  770 QLKKQ 774
Cdd:COG1196   346 LEEAE 350
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
695-779 1.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTE----LEQRIKEAIEKNAQLQslELAHADQLTKEKIEELnKTREEQIQKKQKILEELQKVERELQLKTQQQ 770
Cdd:PRK03918  312 IEKRLSRLEEeingIEERIKELEEKEERLE--ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK 388

                  ....*....
gi 568936357  771 LKKQYLEVK 779
Cdd:PRK03918  389 LEKELEELE 397
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
969-1001 1.64e-03

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: 38.04  E-value: 1.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568936357   969 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 1001
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
1055-1112 1.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936357  1055 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 1112
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
696-777 1.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVER-ELQLKTQQQLKKQ 774
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEElEEAEEALLERLER 418

                  ...
gi 568936357  775 YLE 777
Cdd:COG1196   419 LEE 421
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1954-2205 1.76e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.76  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1954 SPNKGASASEQEASSPPVVEPANSRPPHsssssgsssghstQQQPPGSVPQEPRP--------PLQQSQVPSPDVRMTVP 2025
Cdd:PLN03209  329 PPKESDAADGPKPVPTKPVTPEAPSPPI-------------EEEPPQPKAVVPRPlspytayeDLKPPTSPIPTPPSSSP 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2026 PTATSSAPVAVPSTAPVTyPMPQTQMGCSQPPKMEAPA--------------IRPPSHATAAPHKTPAPVQSSSASVLNV 2091
Cdd:PLN03209  396 ASSKSVDAVAKPAEPDVV-PSPGSASNVPEVEPAQVEAkktrplspyaryedLKPPTSPSPTAPTGVSPSVSSTSSVPAV 474
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2092 NHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGPFSTLFEnnptnahafwgGPVVSSQSTPESMLS 2171
Cdd:PLN03209  475 PDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNE-----------VVKVGNSAPPTALAD 543
                         250       260       270
                  ....*....|....*....|....*....|....
gi 568936357 2172 GKSSYLPNSDPLhqSDTSKAPGFRPPlQRPAPSP 2205
Cdd:PLN03209  544 EQHHAQPKPRPL--SPYTMYEDLKPP-TSPTPSP 574
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1952-2052 1.82e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.55  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1952 SASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVPPTATSS 2031
Cdd:PRK14951  395 AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVAS 474
                          90       100
                  ....*....|....*....|.
gi 568936357 2032 APVAvPSTAPVTYPMPQTQMG 2052
Cdd:PRK14951  475 AAPA-PAAAPAAARLTPTEEG 494
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
972-1023 1.86e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568936357  972 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1023
Cdd:PTZ00322  117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
984-1097 1.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  984 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL---DNGADIEAQSERTKdTPLSLACSGGRQ---EVVELLL 1057
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGF-TMLQVYLQSNHHidiEIIKLLL 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568936357 1058 ARGAN-KEHRNVSDYTPLSLAASGGY----VNIIKILLNAGAEIN 1097
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLHCYFKYNIdridADILKLFVDNGFIIN 213
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
484-512 2.11e-03

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: 37.62  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 568936357   484 GDTALTYACENGHTDVADVLLQAGADLEH 512
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
503-558 2.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   503 LLQAG-ADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLA 558
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
701-780 2.19e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  701 KLTELEQRIKEAIEKN--AQLQSLELAHADQLTKEKIEELNKTREEQIQK-KQKILEELQKVERELQ------LKTQQQL 771
Cdd:cd16269   192 ALTEKEKEIEAERAKAeaAEQERKLLEEQQRELEQKLEDQERSYEEHLRQlKEKMEEERENLLKEQEraleskLKEQEAL 271

                  ....*....
gi 568936357  772 KKQYLEVKA 780
Cdd:cd16269   272 LEEGFKEQA 280
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1007-1261 2.19e-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: 43.53  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1007 LILAATAGHVGVVEILLDNGADIEAQS-ERTKDTPLSLACSGGR-QEVVELLLarganKEHRNVSDYTPLSLAASGGYVN 1084
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1085 ----IIKILLNAGAE------INSRTGSKL--GISPLMLAAMNGHTAAVKLLLDMGSDINAQietnrntaltlAC---FQ 1149
Cdd:TIGR00870   96 aveaILLHLLAAFRKsgplelANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAR-----------ACgdfFV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  1150 GRTEVVSLLLDRkanvehraktglTPLMEAASGGYAEVGRVLLDKGADVNAppvpssRDT-------ALTIAAD-KGHYK 1221
Cdd:TIGR00870  165 KSQGVDSFYHGE------------SPLNAAACLGSPSIVALLSEDPADILT------ADSlgntllhLLVMENEfKAEYE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936357  1222 F----C-ELLIGKGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1261
Cdd:TIGR00870  227 ElscqMyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
692-779 2.19e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   692 ESIVEEAQGKLTELEQR---IKEAIEKNAQLQS--LELahadqltKEKIEELNKTREEQIQKKQKILEELQKVEREL-QL 765
Cdd:TIGR04523  186 QKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESqiSEL-------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLnQL 258
                           90
                   ....*....|....*....
gi 568936357   766 KTQQ-----QLKKQYLEVK 779
Cdd:TIGR04523  259 KDEQnkikkQLSEKQKELE 277
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
701-779 2.24e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  701 KLTELEQRIKEAIEKNAQLQSL--ELAHADQLTKEKIEELNKTRE-----EQIQKKQKILEELQKVERELQLKTQQ--QL 771
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELqeELEELEEELEELEAELEELREeleklEKLLQLLPLYQELEALEAELAELPERleEL 151

                  ....*...
gi 568936357  772 KKQYLEVK 779
Cdd:COG4717   152 EERLEELR 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
237-308 2.33e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357  237 VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLL 308
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
323-539 2.51e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  323 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERgasleevndegytplmeaaREGH 399
Cdd:cd22193    31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  400 eeMVALLLGQGANINAQTeetqetaltlacCGGFLEVADflikAGADIELGcSTPLMEAAQEGHLELVKYLLA---AGAN 476
Cdd:cd22193    91 --IVALLVENGADVHAHA------------KGRFFQPKY----QGEGFYFG-ELPLSLAACTNQPDIVQYLLEnehQPAD 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  477 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHVCTVQFLISK 539
Cdd:cd22193   152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
972-1090 2.73e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  972 TALTLACAGGHEELVQTLLERGASIEHRDKKGF-------------TPLILAATAGHVGVVEILLDNGADIEAQSER--- 1035
Cdd:cd21882    75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdsl 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1036 -----------TKDTP--LSLACSggrqeVVELLLARGANKEH-------RNVSDYTPLSLAASGGYVNIIKILL 1090
Cdd:cd21882   155 gntvlhalvlqADNTPenSAFVCQ-----MYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
PRK12704 PRK12704
phosphodiesterase; Provisional
698-779 2.74e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  698 AQGKLTELEQR----IKEA------IEKNAQLQSLELAH-----ADQLTKEKIEELNKT------REEQIQKKQKILE-- 754
Cdd:PRK12704   29 AEAKIKEAEEEakriLEEAkkeaeaIKKEALLEAKEEIHklrneFEKELRERRNELQKLekrllqKEENLDRKLELLEkr 108
                          90       100
                  ....*....|....*....|....*..
gi 568936357  755 --ELQKVERELQlKTQQQLKKQYLEVK 779
Cdd:PRK12704  109 eeELEKKEKELE-QKQQELEKKEEELE 134
KH-I_IGF2BP2_rpt4 cd22500
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
1617-1681 2.83e-03

fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411928  Cd Length: 78  Bit Score: 38.58  E-value: 2.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDI--DKQKDKTGDRIITIRGGTESTRQATQLINALIK 1681
Cdd:cd22500     6 IKVPSSAAGRVIGKGGKTVNELQNLTSAEVIVprDQTPDENEEVIVKIIGHFFASQTAQRKIREIVQ 72
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
190-216 2.89e-03

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: 37.24  E-value: 2.89e-03
                           10        20
                   ....*....|....*....|....*..
gi 568936357   190 TPLMAAANGGHVKIVKLLLAHKADVNA 216
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
692-895 3.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 766
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  767 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLFTSVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 846
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568936357  847 QALPLATGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 895
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
PHA02859 PHA02859
ankyrin repeat protein; Provisional
285-414 3.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  285 NEFKESALtLACY---KGHLEMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02859   48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357  358 L--TLAACGGHVELAALLIERGASLEEVNDEG----YTPLMeaaREGHEEMVALLLGQGANIN 414
Cdd:PHA02859  127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
290-313 3.37e-03

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: 37.18  E-value: 3.37e-03
                            10        20
                    ....*....|....*....|....
gi 568936357    290 SALTLACYKGHLEMVRFLLEAGAD 313
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGAD 27
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1951-2134 3.49e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1951 GSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRmtvppTATS 2030
Cdd:PRK07003  369 GGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG-----DDAA 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2031 SAPVAVPSTAPVTYPM-PQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPvqSSSASVLNVNHIKRPHSVPSSVQLPSt 2109
Cdd:PRK07003  444 DGDAPVPAKANARASAdSRCDERDAQPPADSGSASAPASDAPPDAAFEPAP--RAAAPSAATPAAVPDARAPAAASRED- 520
                         170       180
                  ....*....|....*....|....*
gi 568936357 2110 lstQSACQNSVHPANKPVAPNFSAP 2134
Cdd:PRK07003  521 ---APAAAAPPAPEARPPTPAAAAP 542
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
692-770 3.55e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 39.44  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQiqkKQKILEELQKV--ERELQLKTQQ 769
Cdd:cd20482     6 QQLLEEARAKIPELRDALKNVEHALSRLQM-QYHKAQNEINETFQFYRSMLEER---KDELLKELESIynAKQLSLNEQQ 81

                  .
gi 568936357  770 Q 770
Cdd:cd20482    82 Q 82
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
662-777 3.70e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 42.11  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   662 RSKAASKQKSNShlpANSQDVQGYItnQSPESIVEEAQGKLTELEQRI----KEAIEKNAQLQSLElahadqltkEKIEE 737
Cdd:pfam15905  165 RNKLEAKMKEVM---AKQEGMEGKL--QVTQKNLEHSKGKVAQLEEKLvsteKEKIEEKSETEKLL---------EYITE 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568936357   738 LNKTREEQIQKKQKI--LEE-LQKVERELQ-LKTQQQLKKQYLE 777
Cdd:pfam15905  231 LSCVSEQVEKYKLDIaqLEElLKEKNDEIEsLKQSLEEKEQELS 274
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
687-777 3.71e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 40.38  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   687 TNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELqlk 766
Cdd:pfam11559   67 EIERLQSKIERLKTQLEDLERELALLQAKERQLEK-KLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREI--- 142
                           90
                   ....*....|.
gi 568936357   767 tqQQLKKQYLE 777
Cdd:pfam11559  143 --EKLKERLAQ 151
rne PRK10811
ribonuclease E; Reviewed
1953-2080 3.78e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1953 ASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQsQVPSPDVrMTVPPTATSSA 2032
Cdd:PRK10811  902 AEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEE-AAETAEV-VVAEPEVVAQP 979
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568936357 2033 PVAVPSTAPVTYPMPQTQMGCSQPPKmEAPAIRPPSHATAAPHKTPAP 2080
Cdd:PRK10811  980 AAPVVAEVAAEVETVTAVEPEVAPAQ-VPEATVEHNHATAPMTRAPAP 1026
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
713-773 3.86e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.47  E-value: 3.86e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357   713 IEKNAQLQSLELAHADQLTK-EKIEELNKTREEQIQKKQKILEE-LQKVE---RELQLKTQQQLKK 773
Cdd:pfam13863    2 LEKKREMFLVQLALDAKREEiERLEELLKQREEELEKKEQELKEdLIKFDkflKENDAKRRRALKK 67
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1617-1676 3.90e-03

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 37.92  E-value: 3.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1617 VSVPSTVISRVIGRGGCNINAIRECTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1676
Cdd:cd22408     4 VEVPKSQHRFVIGPRGSTIQEILEETGCSVEV--PPNDSDSETITLRGPADKLGAALTLV 61
PHA03269 PHA03269
envelope glycoprotein C; Provisional
2038-2192 4.01e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.41  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2038 STAPVTYPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASvlnvnhiKRPHSVPSsvqlpstlstqSACQ 2117
Cdd:PHA03269   18 IIANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRK-------PDLAQAPT-----------PAAS 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 2118 NSVHPANKPVAPNFSAPLPFGPFSTLFENNPTNAHAFWGGPvvssQSTPESMLSGKSSYLPNSDPLHQSDTSKAP 2192
Cdd:PHA03269   80 EKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAEAFTSAA----QAHEAPADAGTSAASKKPDPAAHTQHSPPP 150
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
2163-2349 4.29e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 42.51  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2163 QSTPESMLSGKSSYLPNSDPLHqSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHLGNfASSLSGGQMYGPGA 2242
Cdd:pfam08580  480 QIASTLKQTKRPSKIPRASPNH-SGFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTN-TNDLDVGHNFKPLT 557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  2243 PLGGAPLGGAPTAANfnrqhfSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSS----VSQDR--KVPV 2316
Cdd:pfam08580  558 LTTPSPTPSRSSRSS------STLPPVSPLSRDKSRSPAPTCRSVSRASRRRASRKPTRIGSPNSrtslLDEPPypKLTL 631
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 568936357  2317 PIGTERSARIRQT--GTSA--PSVIGSNL------STSVGHSG 2349
Cdd:pfam08580  632 SKGLPRTPRNRQSyaGTSPsrSVSVSSGLgpqtrpGTSLGSRF 674
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1945-2073 4.30e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.46  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1945 NSPLDCGSASPNKGAsaseQEASSPPVVEPANSRPPHSSSSSGS----SSGHSTQQQPPGSVPQEPRPPlqQSQVPSPDV 2020
Cdd:PRK14971  361 QLTQKGDDASGGRGP----KQHIKPVFTQPAAAPQPSAAAAASPspsqSSAAAQPSAPQSATQPAGTPP--TVSVDPPAA 434
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568936357 2021 RMTVPPTATSsaPVAVPSTAPVTYPMPQTQMGcsqppkMEAPAIRPPSHATAA 2073
Cdd:PRK14971  435 VPVNPPSTAP--QAVRPAQFKEEKKIPVSKVS------SLGPSTLRPIQEKAE 479
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
692-779 4.36e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.79  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  692 ESIVEEAQGKLTELEQRIKEaiEKNAQLQ--------SLElAHADQLTKEKIEELNKTREEQiqkkQKILEELQKVEREL 763
Cdd:cd16269   199 EIEAERAKAEAAEQERKLLE--EQQRELEqkledqerSYE-EHLRQLKEKMEEERENLLKEQ----ERALESKLKEQEAL 271
                          90       100
                  ....*....|....*....|
gi 568936357  764 Q----LKTQQQLKKQYLEVK 779
Cdd:cd16269   272 LeegfKEQAELLQEEIRSLK 291
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
221-252 4.39e-03

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: 36.88  E-value: 4.39e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568936357   221 GNTALTYACA-GGYVDVVKVLLESGASIEDHNE 252
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PRK10905 PRK10905
cell division protein DamX; Validated
1938-2109 4.46e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 41.85  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1938 QPGGVSRNS--PLDCGSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRpplqQSQV 2015
Cdd:PRK10905  113 QLNNVAVNStlPTEPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIEPKKPQATAKTEPKPVAQTPK----RTEP 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2016 PSPDVRMTVPPTATSSAPVAVPSTAPVtypmpqtqmgcsqppkmeapairppshATAAPHKTPAPVQSSSASVLNVNHIK 2095
Cdd:PRK10905  189 AAPVASTKAPAATSTPAPKETATTAPV---------------------------QTASPAQTTATPAAGGKTAGNVGSLK 241
                         170
                  ....*....|....*..
gi 568936357 2096 rphSVPSS---VQLPST 2109
Cdd:PRK10905  242 ---SAPSShytLQLSSS 255
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1616-1676 4.52e-03

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411946 [Multi-domain]  Cd Length: 78  Bit Score: 38.18  E-value: 4.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLI 1676
Cdd:cd22518    10 RLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVagDMLPNST-ERAITIAGIPQSIIECVKQI 71
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1612-1646 4.60e-03

second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) and similar proteins; BICC1, also called Bic-C, is a mammalian homologue of Drosophila Bicaudal-C (dBic-C). BICC1 functions as an RNA-binding protein that represses the translation of selected mRNAs to control development. It regulates gene expression and modulates cell proliferation and apoptosis. BICC1 is a negative regulator of Wnt signaling. Increased levels of BICC1 may be associated with depression. Besides, BICC1 is a genetic determinant of osteoblastogenesis and bone mineral density. BICC1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411849  Cd Length: 70  Bit Score: 37.71  E-value: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568936357 1612 RRSKKVSVPSTVISRVIGRGGCNINAIRECTGAHI 1646
Cdd:cd22421     2 RVTLKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHI 36
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
695-779 4.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIEKNAQLQSLElahaDQLtkEKIEELNKTREEQIQKKQKILEELQKVEREL----------- 763
Cdd:PRK03918  517 LEELEKKAEEYEKLKEKLIKLKGEIKSLK----KEL--EKLEELKKKLAELEKKLDELEEELAELLKELeelgfesveel 590
                          90
                  ....*....|....*...
gi 568936357  764 --QLKTQQQLKKQYLEVK 779
Cdd:PRK03918  591 eeRLKELEPFYNEYLELK 608
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1614-1680 4.70e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 37.95  E-value: 4.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22480     2 TEEYKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQAKRLLGQIV 68
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
983-1125 4.85e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  983 EELVQTLLERG-----------ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERT-------------KD 1038
Cdd:cd22194   110 KEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfGE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1039 TPLSLACSGGRQEVVELLL-----------ARGANKEHR--NVSDytplslaASGGYVNIIK-----ILLNAGAEINSRT 1100
Cdd:cd22194   190 TPLALAACTNQPEIVQLLMekestditsqdSRGNTVLHAlvTVAE-------DSKTQNDFVKrmydmILLKSENKNLETI 262
                         170       180
                  ....*....|....*....|....*
gi 568936357 1101 GSKLGISPLMLAAMNGHTAAVKLLL 1125
Cdd:cd22194   263 RNNEGLTPLQLAAKMGKAEILKYIL 287
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1172-1200 4.94e-03

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: 36.50  E-value: 4.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357  1172 GLTPLMEAA-SGGYAEVGRVLLDKGADVNA 1200
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1072-1207 5.20e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1072 TPLSLAASGGYVNIIKILLNAGAEINSR-----------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNR- 1139
Cdd:cd21882    75 TALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSl 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1140 -NTALTLACFQGR---------TEVVSLLLDRKANVEHRAK-------TGLTPLMEAASGGYAEVGRVLLDKgaDVNAPP 1202
Cdd:cd21882   155 gNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR--EFSGPY 232

                  ....*
gi 568936357 1203 VPSSR 1207
Cdd:cd21882   233 QPLSR 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
1233-1277 5.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568936357  1233 IDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPL 1277
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1051-1195 5.24e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1051 EVVELLLA---------RGANKEHRNvSDY---TPLSLAASGGYVNIIKILLNAGAEINSRT------------GSKLGI 1106
Cdd:cd22194   111 EIVRILLAfaeengildRFINAEYTE-EAYegqTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykheGFYFGE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1107 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNT---ALTLAC--FQGRTEVVSLLLD------RKANVEH-RAKTGLT 1174
Cdd:cd22194   190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAedSKTQNDFVKRMYDmillksENKNLETiRNNEGLT 269
                         170       180
                  ....*....|....*....|....*.
gi 568936357 1175 PLMEAASGGYAEV-----GRVLLDKG 1195
Cdd:cd22194   270 PLQLAAKMGKAEIlkyilSREIKEKP 295
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
704-774 5.56e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 5.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936357   704 ELEQRIKEA---IEKNAQLQSLELAHADQLTKEKieELNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 774
Cdd:pfam13868   10 ELNSKLLAAkcnKERDAQIAEKKRIKAEEKEEER--RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
453-479 5.58e-03

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: 36.47  E-value: 5.58e-03
                           10        20
                   ....*....|....*....|....*..
gi 568936357   453 TPLMEAAQEGHLELVKYLLAAGANVHA 479
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
705-780 5.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 5.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357  705 LEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTrEEQIQKKQKileELQKVERELQlKTQQQLKKQYLEVKA 780
Cdd:COG4372    29 LSEQLRKALFELDKLQE-ELEQLREELEQAREELEQL-EEELEQARS---ELEQLEEELE-ELNEQLQAAQAELAQ 98
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1616-1680 6.00e-03

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411948 [Multi-domain]  Cd Length: 72  Bit Score: 37.69  E-value: 6.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22520     5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVagDLLPNST-ERAVTVSGVPDAIIQCVRQICAVI 70
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
125-210 6.04e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGIKgdiTPLMAAANGGHVK 202
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENGFRE 162

                  ....*...
gi 568936357  203 IVKLLLAH 210
Cdd:PTZ00322  163 VVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1002-1031 6.09e-03

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: 36.47  E-value: 6.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357  1002 KGFTPLILAATAGHVGVVEILLDNGADIEA 1031
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
1951-2329 6.11e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.97  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1951 GSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPP-----GSVPQEPRPPLQQSQVPSPDVRMTVP 2025
Cdd:COG5180   117 ELAAGALPAPAAAAALPKAKVTREATSASAGVALAAALLQRSDPILAKDpdgdsASTLPPPAEKLDKVLTEPRDALKDSP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2026 pTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSsasvlnvnhiKRPHSVPSSVQ 2105
Cdd:COG5180   197 -EKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPE----------MRPPADAKERR 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2106 LPSTLSTQSAcqnsvHPANKPVAPNFSAPLPFGPFSTLFENNPTNAHAFW---GGPVVSSQSTPESMLS--GKSSYLPNS 2180
Cdd:COG5180   266 RAAIGDTPAA-----EPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASAppaTRPVRPPGGARDPGTPrpGQPTERPAG 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2181 DPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHLGNFASSLSGGQMYGPGAPLGGAplgGAPTAANFNR 2260
Cdd:COG5180   341 VPEAASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGA---GDLVQAALDG 417
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 2261 QHFSPLSLLTPCSSASNESPAQSVSSGVRAPS-PAPSSVPLGSEKPSSVSQDRKVPVPIGTERSARIRQT 2329
Cdd:COG5180   418 GGRETASLGGAAGGAGQGPKADFVPGDAESVSgPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGV 487
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
1932-2082 6.20e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.77  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1932 SPSPPAQPGGVSRNSPLDCGSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPgsvPQEPRPPLQ 2011
Cdd:PRK07994  370 VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATK---AKKSEPAAA 446
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 2012 QSQVPSPDVRMTVPPTATSSAPVAVPSTAPVTYPMPQTQmgcsQPPKMEAPAIRPPSHATAAPH-KTPAPVQ 2082
Cdd:PRK07994  447 SRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATN----PVEVKKEPVATPKALKKALEHeKTPELAA 514
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
696-774 6.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 6.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936357  696 EEAQGKLTELEQRIKEAIEKNAQLQSLElahaDQLTKEKiEELNKTREEQIQKKqkilEELQKVERELQLKTQQQLKKQ 774
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAR----EELEQLE-EELEQARSELEQLE----EELEELNEQLQAAQAELAQAQ 100
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
692-780 6.36e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   692 ESIVEEAQGKLTELEQRIKEAIEknaQLQSLELAHADQLtKEKIEELNKT---REEQIQKKQKIL----EELQKVERELQ 764
Cdd:pfam10368   17 EKPFEEQQEPLVELEKKEQELYE---EIIELGMDEFDEI-KKLSDEALENveeREELLEKEKESIeeakEEFKKIKEIIE 92
                           90
                   ....*....|....*.
gi 568936357   765 LKTQQQLKKQYLEVKA 780
Cdd:pfam10368   93 EIEDEELKKEAEELID 108
KH-I_FUBP3_rpt3 cd22486
third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1614-1680 6.48e-03

third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411914  Cd Length: 70  Bit Score: 37.62  E-value: 6.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22486     4 SIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERVAQVMGPPDRCQHAAHIINELI 70
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
696-779 6.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  696 EEAQGKLTELE---QRIKEAIEKNAQL----------QSLELA-HADQLT--KEKIEELN------KTREEQIQKKQKIL 753
Cdd:PRK02224  422 DELREREAELEatlRTARERVEEAEALleagkcpecgQPVEGSpHVETIEedRERVEELEaeledlEEEVEEVEERLERA 501
                          90       100
                  ....*....|....*....|....*..
gi 568936357  754 EELQKVERELQ-LKTQQQLKKQYLEVK 779
Cdd:PRK02224  502 EDLVEAEDRIErLEERREDLEELIAER 528
PHA02798 PHA02798
ankyrin-like protein; Provisional
267-425 6.76e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  267 VEVARLLLENGAGINTHSNEFKESALTLAC----YKGHLEMVRFLLEAGADQEHKTDEMHTALMeaCMdghvevarllLD 342
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY--CL----------LS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  343 SGAQVNMpadsfespltlaacgghvELAALLIERGASLEEVNDEGYTPLMEAAREGHE---EMVALLLGQGANINAQTEE 419
Cdd:PHA02798  119 NGYINNL------------------EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180

                  ....*.
gi 568936357  420 TQETAL 425
Cdd:PHA02798  181 EKYDTL 186
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
696-780 6.79e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   696 EEAQGKLTELEQRIKEA-IEKNAQLQSLElahadqltkekiEELNKTREEQIQKKQKILEELQKVERELQLKTQQQlkKQ 774
Cdd:pfam05672   39 EEERLRKEELRRRAEEErARREEEARRLE------------EERRREEEERQRKAEEEAEEREQREQEEQERLQKQ--KE 104

                   ....*.
gi 568936357   775 YLEVKA 780
Cdd:pfam05672  105 EAEAKA 110
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
708-779 6.83e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 40.31  E-value: 6.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936357  708 RIKEAIEKNAQlqslelAHADQLTKEKIEELNKTREEQIQKKQKILEE-LQKVERELQLKTQQQLKKQYLEVK 779
Cdd:COG1390     6 KIIEEILEEAE------AEAEEILEEAEEEAEKILEEAEEEAEEIKEEiLEKAEREAEREKRRIISSAELEAR 72
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
695-780 6.86e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAIEK----NAQLQSLeLAHADQLTKE----------KIEELNKTREEQIQKKQKIlEELQKVE 760
Cdd:COG1340   169 LKELRKEAEEIHKKIKELAEEaqelHEEMIEL-YKEADELRKEadelhkeiveAQEKADELHEEIIELQKEL-RELRKEL 246
                          90       100
                  ....*....|....*....|...
gi 568936357  761 REL---QLKTQQQLKKQYLEVKA 780
Cdd:COG1340   247 KKLrkkQRALKREKEKEELEEKA 269
PHA02884 PHA02884
ankyrin repeat protein; Provisional
496-602 6.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  496 HTDVADVLLQAGADLEHE---SEGGRT-PLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLL 571
Cdd:PHA02884   45 YTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100       110
                  ....*....|....*....|....*....|.
gi 568936357  572 AHGADPTHRLKDGSTMlIEAAkgghtSVVCY 602
Cdd:PHA02884  125 SYGADINIQTNDMVTP-IELA-----LMICN 149
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
322-348 7.39e-03

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: 36.11  E-value: 7.39e-03
                           10        20
                   ....*....|....*....|....*...
gi 568936357   322 HTALMEAC-MDGHVEVARLLLDSGAQVN 348
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
323-349 7.64e-03

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: 36.08  E-value: 7.64e-03
                           10        20
                   ....*....|....*....|....*..
gi 568936357   323 TALMEACMDGHVEVARLLLDSGAQVNM 349
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1614-1680 7.71e-03

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER and flowering locus K homology domain protein (FLK). PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. The model corresponds to the KH3 domain of PEPPER and FLK.


Pssm-ID: 411889  Cd Length: 69  Bit Score: 37.15  E-value: 7.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357 1614 SKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22461     3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPGEMTVEIHGTQSQVQTAQQLIQNFM 69
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1978-2129 7.94e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1978 RPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPdvrmtvPPTATSSAPVAVPSTAPvtypmpqtqmgcsqPP 2057
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAA------APAAAASAPAAPPAAAP--------------PA 424
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936357 2058 KMEAPAIRPPshaTAAPHKTPAPVQSSSASvlNVNHIKRPHSVPSSVQlPSTLSTQSACQNSVHPANKPVAP 2129
Cdd:PRK14951  425 PVAAPAAAAP---AAAPAAAPAAVALAPAP--PAQAAPETVAIPVRVA-PEPAVASAAPAPAAAPAAARLTP 490
KH-I_AtC3H36_like cd22464
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH ...
1616-1680 8.00e-03

type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH domain-containing proteins AtC3H36, AtC3H52 and similar proteins; The family corresponds to a group of plant CCCH family zinc finger proteins, such as AtC3H36 and AtC3H52, which contain one K homology (KH) RNA-binding domain. They may play important roles in RNA processing as RNA-binding proteins in animals. They may also have an effective role in stress tolerance.


Pssm-ID: 411892 [Multi-domain]  Cd Length: 66  Bit Score: 37.07  E-value: 8.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936357 1616 KVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1680
Cdd:cd22464     2 KISVDASLAGAIIGKGGVNSKQICRETGVKLSIRDHERDPNLKNVELEGSFEQIKEASGMVRELI 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
695-824 8.01e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357  695 VEEAQGKLTELEQRIKEAiekNAQLQSLeLAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQlKTQQQLKKq 774
Cdd:COG4717   158 LRELEEELEELEAELAEL---QEELEEL-LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE-ELEEELEQ- 231
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936357  775 yLEVKAQRIQLQQQQQQSCQHLGLFTSVGVGEQLSEGDYARLQQVDPVLL 824
Cdd:COG4717   232 -LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1239-1268 8.68e-03

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: 35.70  E-value: 8.68e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568936357  1239 KGNTPLWLAANGGHLDVVQLLVQATADVDA 1268
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
701-777 8.79e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.21  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   701 KLTELEQRIKEAIEKNAQLQSlELAHADQLTKE---KIEELNKTREEQ-------IQKKQKILEELQKVeRELQlkTQQQ 770
Cdd:pfam05622  305 RLTELQQLLEDANRRKNELET-QNRLANQRILElqqQVEELQKALQEQgskaedsSLLKQKLEEHLEKL-HEAQ--SELQ 380

                   ....*..
gi 568936357   771 LKKQYLE 777
Cdd:pfam05622  381 KKKEQIE 387
Ank_5 pfam13857
Ankyrin repeats (many copies);
307-361 8.81e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 8.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568936357   307 LLEAG-ADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLA 361
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
696-778 9.49e-03

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 37.96  E-value: 9.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357   696 EEAQGKLTELEQRIKEAIE---KNAQLQSLELAH--ADQLTKEKIEELNKTREEQ-------IQKKQKILEELQKverEL 763
Cdd:pfam14772    8 EQRRRKEEELRRFRKEKLEeeaKSSQEKFEKINQrwRSILRKNKPQELREELEEQkqaceriIDRKDKLIKELQQ---EL 84
                           90
                   ....*....|....*...
gi 568936357   764 QLKTQQ---QLKKQYLEV 778
Cdd:pfam14772   85 KEADEQyvkALRKQAEDI 102
Ank_5 pfam13857
Ankyrin repeats (many copies);
240-295 9.54e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 9.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568936357   240 LLESG-ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLA 295
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1209-1279 9.82e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.28  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936357 1209 TALTIAADKGHYKFCELLIGKGAHIDVRNKK--------------GNTPLWLAANGGHLDVVQLLV-QATADVDAADNRK 1273
Cdd:cd22194   143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMeKESTDITSQDSRG 222

                  ....*.
gi 568936357 1274 ITPLMA 1279
Cdd:cd22194   223 NTVLHA 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH