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Conserved domains on  [gi|530376947|ref|XP_005265730|]
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ankyrin repeat domain-containing protein 17 isoform X11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 9.33e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.61  E-value: 9.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-465 6.85e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  181 AAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSV 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  261 NEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTY 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  341 ACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFL 420
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  421 LEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 7.05e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 7.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 2.78e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 530376947   714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 4.96e-06

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: 47.57  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQslELAHADQLTKEKIEELNKTREEQIQKKQKILEELQ-K 871
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQ--KLYEELQKDGALLEEEREEKEQELQKKEQELQQLQqK 80
                           90       100
                   ....*....|....*....|..
gi 530376947   872 VERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   81 AQQELQKKQQELLQPIQDKINK 102
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1082-1110 2.62e-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: 36.80  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 530376947   1082 NHDTALTLACAGGHEELVQTLLERGASIE 1110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 9.33e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.61  E-value: 9.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-465 6.85e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  181 AAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSV 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  261 NEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTY 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  341 ACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFL 420
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  421 LEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 7.05e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 7.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1152-1438 1.71e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1226
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1227 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1302
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1303 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAA 1382
Cdd:PHA03100  161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530376947 1383 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1438
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03100 PHA03100
ankyrin repeat protein; Provisional
447-625 3.70e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  447 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 519
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  520 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 578
Cdd:PHA03100  128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 530376947  579 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 4.22e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 530376947   385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 8.18e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 8.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 530376947   648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1222-1313 1.02e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1222 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1301
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 530376947  1302 RVLLDKGADVNA 1313
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 7.78e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 7.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 530376947  457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 2.78e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 530376947   714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 9.46e-12

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: 69.66  E-value: 9.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 530376947  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192   177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1145-1374 1.23e-09

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: 62.72  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1145 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 1215
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1216 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1289
Cdd:cd22192    85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1290 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1355
Cdd:cd22192   141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                         250
                  ....*....|....*....
gi 530376947 1356 PLWLAANGGHLDVVQLLVQ 1374
Cdd:cd22192   215 PFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 1.46e-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: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192    21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530376947  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
Cdd:cd22192   180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1069-1305 5.72e-07

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: 5.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1069 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1145
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1146 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1211
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1212 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1264
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 530376947  1265 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 1.02e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 530376947  714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 4.96e-06

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: 47.57  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQslELAHADQLTKEKIEELNKTREEQIQKKQKILEELQ-K 871
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQ--KLYEELQKDGALLEEEREEKEQELQKKEQELQQLQqK 80
                           90       100
                   ....*....|....*....|..
gi 530376947   872 VERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   81 AQQELQKKQQELLQPIQDKINK 102
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
794-893 7.09e-06

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: 47.91  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 869
Cdd:COG2825    30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                          90       100
                  ....*....|....*....|....*
gi 530376947  870 -QKVERELQLKTQQQLKKQYLEVKA 893
Cdd:COG2825   103 qQEAQQDLQKRQQELLQPILEKIQK 127
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-887 8.55e-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: 50.40  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   774 IRNKAASKQKSSSHLPANSQDVQGYITNQSPE--SIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEE 850
Cdd:TIGR04523  326 IQNQISQNNKIISQLNEQISQLKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEK 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530376947   851 LNKTREEQIQKKQKILEELQK-VERELQLKTQQQ-----LKKQ 887
Cdd:TIGR04523  406 LNQQKDEQIKKLQQEKELLEKeIERLKETIIKNNseikdLTNQ 448
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 1.67e-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: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 530376947   442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 2.90e-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: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 530376947   471 LTLAACGGHVELAALLIERGASLE 494
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1352-1381 2.91e-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: 42.19  E-value: 2.91e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 530376947   1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 3.03e-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: 42.19  E-value: 3.03e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 530376947    499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
804-886 4.07e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.28  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  804 PESIVEEAQGKLTELEQRIKEAIEKNAQlQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEE-LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQA 578

                  ...
gi 530376947  884 LKK 886
Cdd:PRK00409  579 IKE 581
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 4.55e-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: 4.55e-04
                            10        20
                    ....*....|....*....|....*....
gi 530376947    334 GNTALTYACAGGYVDVVKVLLESGASIED 362
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-886 1.68e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 1.68e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947    794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 869
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 530376947    870 QKV-ERELQLKTQQQLKK 886
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1082-1110 2.62e-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: 36.80  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 530376947   1082 NHDTALTLACAGGHEELVQTLLERGASIE 1110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1075-1113 4.59e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 4.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530376947  1075 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1113
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
827-887 9.17e-03

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: 36.09  E-value: 9.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947  827 EKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 887
Cdd:cd22249    10 EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 9.33e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.61  E-value: 9.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-699 3.65e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 3.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  414 LEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  494 EEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIEL---GCSTPLME 570
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAqdnDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  571 AAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 650
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947  651 SKGANVNRtTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGST 699
Cdd:COG0666   240 EAGADLNA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-465 6.85e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  181 AAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSV 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  261 NEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTY 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  341 ACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFL 420
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  421 LEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 7.05e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 7.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
353-634 1.43e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  353 LLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTD 432
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  433 EMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGH 512
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  513 EEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGAN 589
Cdd:COG0666   166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgkTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530376947  590 VHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL 634
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1134-1408 8.46e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.44  E-value: 8.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1134 ILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRT 1213
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1214 gsKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAA 1293
Cdd:COG0666    85 --DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1294 SGGYAEVGRVLLDKGADVNAPPvpSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1373
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 530376947 1374 QAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKE 1408
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
314-601 9.14e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 9.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  314 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGI 393
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  394 NThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:COG0666    81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  474 AACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFL 553
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530376947  554 IKAGADIELGC---STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTAL 601
Cdd:COG0666   239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1065-1313 6.29e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 6.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1065 AMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1145 QSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLML 1224
Cdd:COG0666   116 RDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1225 AAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVL 1304
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

                  ....*....
gi 530376947 1305 LDKGADVNA 1313
Cdd:COG0666   272 LLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1066-1357 4.01e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.43  E-value: 4.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1066 MLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1145
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1146 SERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLA 1225
Cdd:COG0666    84 DDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1226 AMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1306 DKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 1357
Cdd:COG0666   240 EAGADLNAK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1164-1407 1.52e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1164 EVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSD 1243
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1244 INAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPvpSSRDTA 1323
Cdd:COG0666    80 INAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1324 LTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1403
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                  ....
gi 530376947 1404 YLVK 1407
Cdd:COG0666   237 LLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-438 5.24e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 5.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  153 LLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQ 232
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  233 SDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGG 312
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  313 HVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAG 392
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 530376947  393 INtHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:COG0666   245 LN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1199-1407 9.68e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 9.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1199 IKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANV 1278
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1279 EHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLW 1358
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947 1359 LAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1152-1438 1.71e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1226
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1227 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1302
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1303 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAA 1382
Cdd:PHA03100  161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530376947 1383 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1438
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
1097-1403 1.01e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.81  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1097 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 1172
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1173 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 1248
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1249 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1324
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947 1325 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1403
Cdd:PHA03095  253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
447-625 3.70e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  447 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 519
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  520 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 578
Cdd:PHA03100  128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 530376947  579 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
240-560 1.55e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.88  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  240 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 315
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  316 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 389
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  390 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 456
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  457 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 535
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 530376947  536 TA----LTLACCGGFLEVADFLIKAGADI 560
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 4.22e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 530376947   385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
238-623 6.18e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 6.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDV--NAVRKLLIEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVEDRGIKGdITPLMAAANGGHVK 315
Cdd:PHA02876  125 LKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADVNAKDIYC-ITPIHYAAERGNAK 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  316 IVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIedhNENGHTpLMEAGSAGHVEVARLLLENGAGINT 395
Cdd:PHA02876  193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDLETSLLLYDAGFSVNS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  396 hSNEFKESALTLACYKGHL-EMVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:PHA02876  269 -IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQ 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  474 AAC-GGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGG--FLEVA 550
Cdd:PHA02876  348 ASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTnpYMSVK 426
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947  551 DfLIKAGADIELG---CSTPLMEAAQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTDVADVLLQAGADL 623
Cdd:PHA02876  427 T-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 8.18e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 8.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 530376947   648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
396-704 5.11e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 5.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  396 HSNEFKESAL---TLACYKGHLEMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 468
Cdd:PHA03095    6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  469 SPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAAR--EGHEEMVALLLGQGANINAqTEETQETALtlaccgg 545
Cdd:PHA03095   85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNA-LDLYGMTPL------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  546 flevADFLIKAGADIELgcstplmeaaqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 623
Cdd:PHA03095  157 ----AVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  624 EHESEGGRTPLMKAArAGHVCT---VQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 700
Cdd:PHA03095  216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                  ....
gi 530376947  701 LIEA 704
Cdd:PHA03095  294 LSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
289-528 5.75e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 5.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  289 MHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYV-----DVVKVLLESGASIEDH 363
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  364 NENGHTPLMEAGSA--GHVEVARLLLENGAGINTHSNEFKES-ALTLACYKGHLEMVRFLLEAGADQEHKTDemhtalme 440
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  441 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:PHA03100  175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                  ....*...
gi 530376947  521 GQGANINA 528
Cdd:PHA03100  246 NNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1098-1394 7.63e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 7.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1098 LVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIE------------AQSERTKDT------------- 1152
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDSKNIDTikaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1153 -PLSL--ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMN 1228
Cdd:PHA02876  240 nDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKN 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1229 GH-TAAVKLLLDMGSDINAQiETNRNTALTLACFQGR-TEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLD 1306
Cdd:PHA02876  318 GYdTENIRTLIMLGADVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1307 KGADVNAppVPSSRDTALTIA-ADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1384
Cdd:PHA02876  397 YGADIEA--LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINI 474
                         330
                  ....*....|
gi 530376947 1385 RKITPLMAAF 1394
Cdd:PHA02876  475 QNQYPLLIAL 484
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1096-1280 1.50e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1096 EELVQTLLERGASIEHRDKKGFTPLILAATAGHV-----GVVEILLDNGADIEAQSERTkDTPLSLACSGGRQ--EVVEL 1168
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKKSNsySIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1169 LLARGANKEHRNVSDYTPLSLAASGGYV--NIIKILLNAGAEINSRT--------GSKL------GISPLMLAAMNGHTA 1232
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsyGVPInikdvyGFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 530376947 1233 AVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVVSLLLDRKANVEH 1280
Cdd:PHA03100  207 FVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
438-529 6.45e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 6.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   438 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASleEVNDEGYTPLMEAAREGHEEMVA 517
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 530376947   518 LLLGQGANINAQ 529
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1097-1250 9.39e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 9.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1097 ELVQTLLERGASIEHRDKKGFTPLILAATA--GHVGVVEILLDNGADIEAQSERTKdTPLSLACSGGRQ--EVVELLLAR 1172
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIdlKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1173 GA--NKEHR--------------NVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKL 1236
Cdd:PHA03100  166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|....
gi 530376947 1237 LLDMGSDINAQIET 1250
Cdd:PHA03100  244 LLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1222-1313 1.02e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1222 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1301
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 530376947  1302 RVLLDKGADVNA 1313
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
312-634 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  312 GHVKIVKLLLAHKAD-VNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  391 agINThsnefkeSALTLACYKGhlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02874   92 --VDT-------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQteetqetaltlaCCGGFleva 550
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  551 dflikagadielgcsTPLMEAAQegHLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHE 626
Cdd:PHA02874  225 ---------------TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIK 284

                  ....*...
gi 530376947  627 SEGGRTPL 634
Cdd:PHA02874  285 DNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
338-430 4.52e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 4.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   338 LTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENgagINTHSNEFKESALTLACYKGHLEMV 417
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 530376947   418 RFLLEAGADQEHK 430
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
349-719 5.82e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.20  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  349 VVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEfKESALTLACYKGHLEMVRFLLeagaDQE 428
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  429 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGASLEEVNDEGYTPLMEA 507
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  508 AREGHE-EMVALLLGQGANINAqteetqetaltlaccggflevADFLIkagadielgcSTPLMEAAQ-EGHLELVKYLLA 585
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  586 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-VCTVQFLISKGANVNrtTANND 664
Cdd:PHA02876  364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  665 -HTVLSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTSVVCYLLDY 719
Cdd:PHA02876  442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 7.78e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 7.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 530376947  457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
346-652 1.11e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  346 YVDVVKVLLESGASIEDHNENGHTPL---MEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLE 422
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  423 AGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGASLE 494
Cdd:PHA03095  106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  495 EVNDEGYTPLmeaaregheemvalllgqgaNINAQTEETQETaltlaccggfleVADFLIKAGAD---IELGCSTPLMEA 571
Cdd:PHA03095  182 AVDDRFRSLL--------------------HHHLQSFKPRAR------------IVRELIRAGCDpaaTDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  572 AQEGHLE--LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA03095  230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                  ...
gi 530376947  650 ISK 652
Cdd:PHA03095  310 LAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
371-461 1.17e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   371 LMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 450
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 530376947   451 RLLLDSGAQVN 461
Cdd:pfam12796   78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1187-1281 2.76e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1187 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKLLLDMgsdINAQIETNRNTALTLACFQGRTE 1266
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 530376947  1267 VVSLLLDRKANVEHR 1281
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-593 6.13e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 6.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   504 LMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGGFLEVADFLI-KAGADIELGCSTPLMEAAQEGHLELVKY 582
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|.
gi 530376947   583 LLAAGANVHAT 593
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
601-693 7.52e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 7.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   601 LTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKgANVNRTtaNNDHTVLSLACAGGHLAVV 680
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK--DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 530376947   681 ELLLAHGADPTHR 693
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1126-1455 1.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.71  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1126 AGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNA 1205
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1206 GAEinsrtgsklgISPLMLAAMNGHTaaVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTG 1285
Cdd:PHA02874   91 GVD----------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1286 LTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA----- 1360
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnr 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1361 ----------------ANGG-----------HLDVVQLLVQAGADVDAADNRKITPLMAAFRK-GHVKVVR------YLV 1406
Cdd:PHA02874  236 saiellinnasindqdIDGStplhhainppcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLI 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947 1407 KEVNQFPsDSECMRYIATITDKEMLKKCHLCMESIVQAKdRQAAEANKN 1455
Cdd:PHA02874  316 KEADKLK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK-KTKCGCDKN 362
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1085-1277 1.16e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQE 1164
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1165 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHTAAVKLLLDMGSDI 1244
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 530376947 1245 NAqieTNRNTALTLACF---QGRTEVVSLLLDRKAN 1277
Cdd:PHA02875  195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1154-1247 1.67e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1154 LSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHTAA 1233
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 530376947  1234 VKLLLDMGSDINAQ 1247
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1087-1180 1.93e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1087 LTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNgADIEAQSErtKDTPLSLACSGGRQEVV 1166
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 530376947  1167 ELLLARGANKEHRN 1180
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
1073-1316 2.97e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1073 IDIDAqTESNHDTAL-TLACAGGHEELVQTLLERGASIEHRDKKGFTPL--ILAATAGHVGVVEILLDNGADIEAQSERT 1149
Cdd:PHA03095   74 ADVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1150 KdTPLS--------------LACSGG-----------------------RQEVVELLLARGANKEHRNVSDYTPLSLAAS 1192
Cdd:PHA03095  153 M-TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1193 GGYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrNTALTLACFQGRTEVVSL 1270
Cdd:PHA03095  232 GSSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRA 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530376947 1271 LLDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1316
Cdd:PHA03095  309 ALAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-562 5.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 5.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLgQGANINAQTEetQETALTLACCGGFLEVA 550
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 530376947   551 DFLIKAGADIEL 562
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1324-1407 8.49e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 8.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1324 LTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQaGADVDAADNRKiTPLMAAFRKGHVKVVR 1403
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....
gi 530376947  1404 YLVK 1407
Cdd:pfam12796   79 LLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
514-727 1.45e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  514 EMVALLLGQGANINaQTEETQETALT--LAC-CGGFLEVADFLIKAGADI---ELGCSTPL---MEAAQEghLELVKYLL 584
Cdd:PHA03095   28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVnapERCGFTPLhlyLYNATT--LDVIKLLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  585 AAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHVCTVQFLISKGANVnRT 659
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADV-YA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  660 TANNDHTVLSLacaggHL-------AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTSVVCYLL------DYPNNLL 724
Cdd:PHA03095  183 VDDRFRSLLHH-----HLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLiagisiNARNRYG 257

                  ...
gi 530376947  725 SAP 727
Cdd:PHA03095  258 QTP 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1289-1383 2.36e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 2.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1289 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIgrgAHIDVRNK-KGNTPLWLAANGGHLD 1367
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 530376947  1368 VVQLLVQAGADVDAAD 1383
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
305-473 6.22e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 6.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  385 LLLENGAGINTHSNefkESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVN-MP 463
Cdd:PLN03192  609 ILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkAN 685
                         170
                  ....*....|
gi 530376947  464 ADSFESPLTL 473
Cdd:PLN03192  686 TDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-330 1.65e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGikgdITPLMAAANGGHVKI 316
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG----RTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 530376947   317 VKLLLAHKADVNAQ 330
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1256-1350 2.11e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 2.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1256 LTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1335
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 530376947  1336 CELLIGRGAHIDVRN 1350
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
337-559 2.42e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  337 ALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEM 416
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  417 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLE 494
Cdd:PHA02875   84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530376947  495 EVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGAD 559
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
1266-1407 2.46e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.45  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1266 EVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC------ 1336
Cdd:PHA03095   28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnattld 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947 1337 --ELLIGRGAHIDVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADVDAADNRKITPLmAAFRKGH---VKVVRYLVK 1407
Cdd:PHA03095   99 viKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
246-442 4.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  246 DVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKA 325
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  326 DVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESAL 405
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530376947  406 TLACYKGHLEMVRFLLEAGADQEHKT---DEMHTALMEAC 442
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
437-689 6.07e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  437 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAsLEEVNDEGY-TPLMEAAREGHEEM 515
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  516 VALLLGQGANINaqteetqetaltlaccggflevaDFLIKAGadielgcSTPLMEAAQEGHLELVKYLLAAGANVHATTA 595
Cdd:PHA02875   84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  596 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGG 675
Cdd:PHA02875  134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
                         250
                  ....*....|....
gi 530376947  676 HLAVVELLLAHGAD 689
Cdd:PHA02875  214 KIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
478-742 9.52e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 9.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  478 GHVELAALLIE-RGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTlACCGGFLEVADFLIKA 556
Cdd:PHA02874   12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  557 GADIELgCSTPLMEAaqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 636
Cdd:PHA02874   91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  637 AARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLiEAAKGGHTSVVCYL 716
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL-HNAIIHNRSAIELL 241
                         250       260
                  ....*....|....*....|....*.
gi 530376947  717 LdypnNLLSAPPPDVTQLTPPSHDLN 742
Cdd:PHA02874  242 I----NNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1097-1396 1.10e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.38  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1097 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVGVVEILLDNGADIEAQSERTkdtpLSLACSGGRQEVVELLLARGAN 1175
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA----IKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1176 KEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrN 1253
Cdd:PHA02878  127 NIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-N 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1254 TALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVLLDKGADVNAppvpssRDTALTIAAdk 1330
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYILGLTA-- 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530376947 1331 ghykfcelligrgAHIDVRNKkgntplwlaangghlDVVQLLVQAGADVDAADNRKITPLMAAFRK 1396
Cdd:PHA02878  273 -------------LHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1152-1344 2.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHT 1231
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1232 AAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1311
Cdd:PHA02875  116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530376947 1312 N----APPVpssrdTALTIAADKGHYKFCELLIGRGA 1344
Cdd:PHA02875  195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1157-1378 3.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1157 ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHTAAVK 1235
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1236 LLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1315
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530376947 1316 VPSSrdTALTIAADKGHYKFCELLIGRGAHIDVRNKKGN-TPLWLAANGGHLDVVQLLVQAGAD 1378
Cdd:PHA02875  166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
271-491 1.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  271 LCLACSAGYYELAQVLLAMHANvEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGIN-PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  351 KVLLESGASIED-HNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PHA02875   85 EELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530376947  430 KTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAdsfESPLTLAACGG----HVELAALLIERGA 491
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG---KNGCVAALCYAiennKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1190-1407 2.09e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1190 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVS 1269
Cdd:PHA02875    9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1270 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIGRGAHID 1347
Cdd:PHA02875   86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947 1348 VRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRK-ITPLMAAFRKGHVKVVRYLVK 1407
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 2.78e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 530376947   714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
312-540 2.78e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  312 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGAsIEDHNENG-HTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  391 AGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02875   92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947  471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHE-EMVALLLGQGANINAQTEETQETALTL 540
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTIL 242
PHA02874 PHA02874
ankyrin repeat protein; Provisional
449-684 1.36e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  449 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGAN--I 526
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  527 NAQTEETQETALTLACCGGFLEVADFLIKagadielgcsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACE 606
Cdd:PHA02874   97 LPIPCIEKDMIKTILDCGIDVNIKDAELK----------TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  607 NGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHlAVVELLL 684
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1165-1406 1.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1165 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDI 1244
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1245 NAQ----IETNRNTALtlacfqgrtEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 1319
Cdd:PHA02876  238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1320 rDTALTIAADKGH-YKFCELLIGRGAHIDVRNKKGNTPLWLAAN-GGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKG 1397
Cdd:PHA02876  308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                  ....*....
gi 530376947 1398 HVKVVRYLV 1406
Cdd:PHA02876  387 NVVIINTLL 395
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1131-1305 1.44e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1131 VVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1211 SRtgSKLGISPLMLAAMNGHTAAV-KLLLDMGSDINAQIETNRNTALTLACFQGRteVVSLLLDRKANVEHRAKTGLTPL 1289
Cdd:PHA02878  229 AR--DKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPL 304
                         170
                  ....*....|....*..
gi 530376947 1290 MEAASGGYA-EVGRVLL 1305
Cdd:PHA02878  305 SSAVKQYLCiNIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
482-749 1.65e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  482 LAALLIERGASLEE---VNDEGYTPLMEAAREGHEEMVALLLGQ--GANINAQTEETQET-ALTLACCG--GFLEVadfL 553
Cdd:PLN03192  468 LSQLLRLKTSTLIEamqTRQEDNVVILKNFLQHHKELHDLNVGDllGDNGGEHDDPNMASnLLTVASTGnaALLEE---L 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  554 IKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAgADLEHESEGG 630
Cdd:PLN03192  545 LKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAG 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  631 RTpLMKAARAGHVCTVQFLISKGANVNrttaNNDH---TVLSLACAGGHLAVVELLLAHGADPTHRLKD---GSTMLIEA 704
Cdd:PLN03192  624 DL-LCTAAKRNDLTAMKELLKQGLNVD----SEDHqgaTALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELREL 698
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947  705 AK----GGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPV 749
Cdd:PLN03192  699 LQkrelGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI 747
PHA02878 PHA02878
ankyrin repeat protein; Provisional
236-426 1.72e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  236 RSLAEACSEGDVNAVRKLLIegrsvNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGIKGDITPLMAAAN 310
Cdd:PHA02878  103 VAIKDAFNNRNVEIFKIILT-----NRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  311 GGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL-MEAGSAGHVEVARLLLEN 389
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530376947  390 GAGINTHSNEFKESALTLACYKGhlEMVRFLLEAGAD 426
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1039-1311 2.60e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1039 NTPTHSIAasisqpQTPtpspiiSPSAMLP--IYPAIDIDAQTESNhDTALTLACAGGHE-ELVQTLLERGASIEHRDKK 1115
Cdd:PHA02876  274 NTPLHHAS------QAP------SLSRLVPklLERGADVNAKNIKG-ETPLYLMAKNGYDtENIRTLIMLGADVNAADRL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1116 GFTPLILAATaghvgvveilLDngadieaqseRTKDTPLSlacsggrqevvelLLARGANKEHRNVSDYTPLSLAASGGY 1195
Cdd:PHA02876  341 YITPLHQAST----------LD----------RNKDIVIT-------------LLELGANVNARDYCDKTPIHYAAVRNN 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1196 VNIIKILLNAGAEINSRTgSKLGIS-PLMLAAMNGHTaAVKLLLDMGSDINAQiETNRNTALTLACFQG-RTEVVSLLLD 1273
Cdd:PHA02876  388 VVIINTLLDYGADIEALS-QKIGTAlHFALCGTNPYM-SVKTLIDRGANVNSK-NKDLSTPLHYACKKNcKLDVIEMLLD 464
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530376947 1274 RKANVEHRAKTGLTPLMEAAsgGYAEVGRVLLDKGADV 1311
Cdd:PHA02876  465 NGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
447-627 2.97e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  447 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGASLEEVND-EGYTPLMEAAREGHEEMVALLLGQGAN 525
Cdd:PLN03192  507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  526 INAQtEETQETALTLACCGGFLEVADFLIK--------AGADIelgcstpLMEAAQEGHLELVKYLLAAGANVHATTATG 597
Cdd:PLN03192  584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
                         170       180       190
                  ....*....|....*....|....*....|
gi 530376947  598 DTALTYACENGHTDVADVLLQAGADLEHES 627
Cdd:PLN03192  656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1251-1407 6.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 6.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1251 NRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1328
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1329 DKGHYKFCELLIGRGAHI-DVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:PHA02875   77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 9.46e-12

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: 69.66  E-value: 9.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 530376947  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192   177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
PHA02878 PHA02878
ankyrin repeat protein; Provisional
347-639 1.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  347 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLengAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGAD 426
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  427 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTP 503
Cdd:PHA02878  127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  504 LMEAAREGHEEMVALLLGQGANINAQTEetqetaltlacCGgflevadflikagadielgcSTPL-MEAAQEGHLELVKY 582
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  583 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 639
Cdd:PHA02878  254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1069-1145 2.51e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 2.51e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947  1069 IYPAIDIDAQTEsNHDTALTLACAGGHEELVQTLLERgASIEHRDkKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1145
Cdd:pfam12796   17 LENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
304-560 3.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  304 PLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgaSIEDHNENGHTPLMEAGSAGHVEVA 383
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  384 RLLLengagINTHSNEfKESALTLACYKGH-----LEMVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 457
Cdd:PHA02878  118 KIIL-----TNRYKNI-QTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  458 AQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL-MEAAREGHEEMVALLLGQGANINAQTEETQET 536
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
                         250       260
                  ....*....|....*....|....
gi 530376947  537 ALTLACCGGflEVADFLIKAGADI 560
Cdd:PHA02878  272 ALHSSIKSE--RKLKLLLEYGADI 293
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-354 3.91e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 3.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947   303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLL 354
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
369-584 5.44e-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: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  369 TPLMEAGSAGHVE-VARLLLENGAGINTHSnEFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMH---TALMEAC 442
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  443 MDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL---- 504
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  505 MEAAREGHEEMVALLLGQGANINAQTEETQETALTLaccggflevadflikagadielgcsTPLMEAAQEGHLELVKYLL 584
Cdd:cd22192   178 LQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGL-------------------------TPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
564-617 7.11e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 7.11e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947   564 CSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 617
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1220-1383 1.12e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1299
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1300 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADV 1379
Cdd:PLN03192  606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                  ....
gi 530376947 1380 DAAD 1383
Cdd:PLN03192  682 DKAN 685
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1357-1411 1.52e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.52e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376947  1357 LWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQ 1411
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
229-407 2.10e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  229 NAGQSDNRSLAE----ACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTP 304
Cdd:PLN03192  516 NGGEHDDPNMASnlltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TA 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  305 LMAAANGGHVKIVKLLLAHKADVNAQssTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  595 LWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180
                  ....*....|....*....|....
gi 530376947  385 LLLENGAGInTHSNEFKE-SALTL 407
Cdd:PLN03192  673 LLIMNGADV-DKANTDDDfSPTEL 695
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
303-429 3.38e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgASIEDHNENGHTpLMEAGSAGHVEV 382
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTA 637
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530376947  383 ARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
245-366 3.66e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  245 GDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR-------GIKGDI------TPLMA 307
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsyGVPINIkdvygfTPLHY 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947  308 AANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNEN 366
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1176-1390 3.92e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1176 KEHR----NVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKlGISPLMLAAMNGHTAAVKLLLdmgSDINAQIETN 1251
Cdd:PHA02878   26 TENYstsaSLIPFIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHR-DLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1252 RNTALTLACFQGRTEVV-SLLLDRKANVEhraKTGLTPLMEAASGGY--AEVGRVLLDKGADVNAPPvPSSRDTALTIAA 1328
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIFkIILTNRYKNIQ---TIDLVYIDKKSKDDIieAEITKLLLSYGADINMKD-RHKGNTALHYAT 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1329 DKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1092-1170 1.01e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947 1092 AGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAqSERTKDTPLSLACSGGRQEVVELLL 1170
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
238-398 1.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----------------AMHANVEDRGIKGD 301
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekDMIKTILDCGIDVN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  302 I------TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAG 375
Cdd:PHA02874  119 IkdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         170       180
                  ....*....|....*....|...
gi 530376947  376 SAGHVEVARLLLENGAGINTHSN 398
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCK 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
1353-1406 1.05e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947  1353 GNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLV 1406
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1145-1374 1.23e-09

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: 62.72  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1145 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 1215
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1216 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1289
Cdd:cd22192    85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1290 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1355
Cdd:cd22192   141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                         250
                  ....*....|....*....
gi 530376947 1356 PLWLAANGGHLDVVQLLVQ 1374
Cdd:cd22192   215 PFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
238-510 1.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSA----GYYELAQVLLAMHANVEDRGIKgditplmAAANGGH 313
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIK-------DAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  314 VKIVKLLLAHKADVNAQSStgntaLTYACAGGYVD-----VVKVLLESGASIEDHNEN-GHTPLMEAGSAGHVEVARLLL 387
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTID-----LVYIDKKSKDDiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  388 ENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEA---CMDghVEVARLLLDSGAQVNmpA 464
Cdd:PHA02878  189 SYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVN--A 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 530376947  465 DSFESPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAARE 510
Cdd:PHA02878  264 KSYILGLTALHSSIKSErKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
1083-1136 2.36e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.36e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947  1083 HDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1136
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
314-531 2.70e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  314 VKIVKLLLAHKADVNAQSSTGNTALT--------YACAggyVDVVKVLLESGASIEDHNENGHTP---LMEAGSAGHVEV 382
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnikdYKHM---LDIVKILIENGADINKKNSDGETPlycLLSNGYINNLEI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  383 ARLLLENGAGINTHSNeFKESALTLACYKGH---LEMVRFLLEAGAD-----QEHKTDEMHTALME--ACMDghVEVARL 452
Cdd:PHA02798  128 LLFMIENGADTTLLDK-DGFTMLQVYLQSNHhidIEIIKLLLEKGVDinthnNKEKYDTLHCYFKYniDRID--ADILKL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  453 LLDSGAQVNMPADSFESPL-----TLAACGGHVELAAL-LIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANI 526
Cdd:PHA02798  205 FVDNGFIINKENKSHKKKFmeylnSLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDI 284

                  ....*
gi 530376947  527 NAQTE 531
Cdd:PHA02798  285 NIITE 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1085-1204 6.46e-09

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: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1085 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 1150
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947 1151 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1204
Cdd:cd22192   170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
1320-1373 7.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 7.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947  1320 RDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1373
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1241-1406 7.20e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 7.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1241 GSDINAQIETNRNTALTLacfqGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1320
Cdd:PLN03192  518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1321 DTALTIAADKGHYKFCELLIgRGAHIDVRNKKGNTpLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVK 1400
Cdd:PLN03192  592 NTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                  ....*.
gi 530376947 1401 VVRYLV 1406
Cdd:PLN03192  670 MVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-387 1.08e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947   334 GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
666-717 1.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947   666 TVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 717
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
597-650 1.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947   597 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 650
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
367-421 1.32e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376947   367 GHTPLMEAGSAGHVEVARLLLENGAGINtHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
346-731 1.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  346 YVDVVKVLLESGASIeDHNENGHT--------PLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYK----GH 413
Cdd:PHA02878    9 YTDNYETILKYIEYI-DHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEpnklGM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  414 LEMVRFLLEAGADQEHKtdemhtALMEACMDGHVEVARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGASL 493
Cdd:PHA02878   87 KEMIRSINKCSVFYTLV------AIKDAFNNRNVEIFKIIL---------TNRYKN------------------IQTIDL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  494 EEVNDEGYTPLMEAaregheEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcSTPLMEAAQ 573
Cdd:PHA02878  134 VYIDKKSKDDIIEA------EITKLLLSYGADINMKDRHKG------------------------------NTALHYATE 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  574 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL-MKAARAGHVCTVQFLISK 652
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947  653 GANVNRTTANNDHTVLSLACAGGHlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDV 731
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
Ank_2 pfam12796
Ankyrin repeats (3 copies);
668-721 1.76e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.76e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947   668 LSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPN 721
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1189-1291 2.67e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1189 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVV 1268
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 530376947 1269 SLLL-------DRKANVEHRAKTGLTPLME 1291
Cdd:PTZ00322  165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
PHA02989 PHA02989
ankyrin repeat protein; Provisional
314-618 4.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  314 VKIVKLLLAHKADVNAQS--STGNTAL---TYACAGGYVDVVKVLLESGASIEDHNENGHTPLM---EAGSAGHVEVARL 385
Cdd:PHA02989   50 IKIVKLLIDNGADVNYKGyiETPLCAVlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  386 LLENGAGINTHSNE--FKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVArllldsgaqvnmp 463
Cdd:PHA02989  130 LLSKGINVNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVI------------- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  464 adsfespltlaacggHVELAALLIERGASLEEvNDEGYTPLMEAAREGHEEMValllgqganinaqteeTQEtaltlacc 543
Cdd:PHA02989  197 ---------------SIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------------KKE-------- 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  544 ggfLEVADFL---IKAGADIELGCsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQ 618
Cdd:PHA02989  237 ---FKVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
469-520 4.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.58e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947   469 SPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
434-487 4.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947   434 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 487
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1074-1262 9.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1074 DIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSeRTKDTP 1153
Cdd:PHA02878  159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1154 LSLACSggrqevvelllargankehrNVSDYtplslaasggyvNIIKILLNAGAEINSRTgSKLGISPLMLAAMNghTAA 1233
Cdd:PHA02878  238 LHISVG--------------------YCKDY------------DILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERK 282
                         170       180
                  ....*....|....*....|....*....
gi 530376947 1234 VKLLLDMGSDINAqIETNRNTALTLACFQ 1262
Cdd:PHA02878  283 LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1164-1402 9.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1164 EVVELLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAV--- 1234
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1235 KLLLDMGSDINAQIETNRNTAL--TLACFQGRTEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1307
Cdd:PHA02989  128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1308 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADN 1384
Cdd:PHA02989  208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
                         250
                  ....*....|....*...
gi 530376947 1385 RKITPLMAAFRKGHVKVV 1402
Cdd:PHA02989  288 DGDTVLTYAIKHGNIDML 305
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
308-387 1.01e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  308 AANGGHVKIvKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:PTZ00322   90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 1.46e-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: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192    21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530376947  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
Cdd:cd22192   180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
500-554 1.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376947   500 GYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLI 554
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1220-1407 2.28e-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: 55.40  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1294
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1295 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLwlaan 1362
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1363 ggHLDVVQ------------LLVQAGADVDAA-----DNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:cd22192   174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-684 2.62e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376947   630 GRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLL 684
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-454 3.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 3.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947   403 SALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 454
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1079-1258 3.26e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1079 TESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQsERTKDTPLSLAC 1158
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1159 SGGRQEVVELLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLL 1238
Cdd:PLN03192  600 SAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLI 675
                         170       180
                  ....*....|....*....|
gi 530376947 1239 DMGSDINAQIETNRNTALTL 1258
Cdd:PLN03192  676 MNGADVDKANTDDDFSPTEL 695
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1069-1305 5.72e-07

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: 5.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1069 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1145
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1146 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1211
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1212 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1264
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 530376947  1265 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 1.02e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 530376947  714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
1220-1272 1.12e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530376947  1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLL 1272
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1352-1384 1.18e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 1.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 530376947  1352 KGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1384
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1233-1434 1.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1233 AVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRA--KTGLTPLM---EAASGGYAEVGRVLLDK 1307
Cdd:PHA02989   18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1308 GADVNAPPVPSSRDTALTIAadKGHYKFCE---LLIGRGAHI-DVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADV-D 1380
Cdd:PHA02989   98 GADINLKTFNGVSPIVCFIY--NSNINNCDmlrFLLSKGINVnDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530376947 1381 AADNRKITPLMAAFRKG----HVKVVRYLVK-----EVNQFPSDSECMRYIAtiTDKEMLKKC 1434
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKkgvniETNNNGSESVLESFLD--NNKILSKKE 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
1272-1407 1.29e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1272 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIGRGAHIDV 1348
Cdd:PHA03095    1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530376947 1349 RNKKGNTPLWL-AANGGHLDVVQLLVQAGADVDAADNRKITPL---MAAFRKgHVKVVRYLVK 1407
Cdd:PHA03095   79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
436-652 2.62e-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: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  436 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIErgASLEEVND-------EGYTPLMEA 507
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  508 AREGHEEMVALLLGQGANInaqteetqetaLTLACCGGFlevadFLIKAGADIELGcSTPLMEAAQEGHLELVKYLLAAG 587
Cdd:cd22192    97 VVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  588 ANVHATTATGDTAL---------TYACEnghtdVADVLL-----QAGADLEHESEG-GRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22192   160 ADIRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1131-1313 2.63e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1131 VVEILLDNGadiEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:PLN03192  509 VGDLLGDNG---GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1211 SRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrntALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLM 1290
Cdd:PLN03192  586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                         170       180
                  ....*....|....*....|...
gi 530376947 1291 EAASGGYAEVGRVLLDKGADVNA 1313
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVDK 683
Ank_5 pfam13857
Ankyrin repeats (many copies);
1102-1157 2.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947  1102 LLERG-ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLA 1157
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1289-1372 4.72e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1289 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGG 1364
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                  ....*...
gi 530376947 1365 HLDVVQLL 1372
Cdd:PTZ00322  160 FREVVQLL 167
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1218-1374 4.88e-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: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1218 GISPLMLAAMN---GHTAAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRTEVVSLLLDRKANVEHRA-- 1282
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1283 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1338
Cdd:cd21882   106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530376947 1339 LIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1374
Cdd:cd21882   183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 4.96e-06

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: 47.57  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQslELAHADQLTKEKIEELNKTREEQIQKKQKILEELQ-K 871
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQ--KLYEELQKDGALLEEEREEKEQELQKKEQELQQLQqK 80
                           90       100
                   ....*....|....*....|..
gi 530376947   872 VERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   81 AQQELQKKQQELLQPIQDKINK 102
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
371-475 5.64e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  371 LMEAGSAGHVEVARLLLENGAgiNTHSNEFKESA-LTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 449
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530376947  450 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 475
Cdd:PTZ00322  164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
PHA02875 PHA02875
ankyrin repeat protein; Provisional
568-719 5.65e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQ 647
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947  648 FLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDY 719
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
1184-1238 6.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 6.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530376947  1184 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLL 1238
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
423-521 6.09e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  423 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:PTZ00322   62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                          90       100
                  ....*....|....*....|....*...
gi 530376947  494 EEVNDEGYTPLMEAAREGHEEMVALLLG 521
Cdd:PTZ00322  142 TLLDKDGKTPLELAEENGFREVVQLLSR 169
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
794-893 7.09e-06

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: 47.91  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 869
Cdd:COG2825    30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                          90       100
                  ....*....|....*....|....*
gi 530376947  870 -QKVERELQLKTQQQLKKQYLEVKA 893
Cdd:COG2825   103 qQEAQQDLQKRQQELLQPILEKIQK 127
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-887 8.55e-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: 50.40  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   774 IRNKAASKQKSSSHLPANSQDVQGYITNQSPE--SIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEE 850
Cdd:TIGR04523  326 IQNQISQNNKIISQLNEQISQLKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEK 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530376947   851 LNKTREEQIQKKQKILEELQK-VERELQLKTQQQ-----LKKQ 887
Cdd:TIGR04523  406 LNQQKDEQIKKLQQEKELLEKeIERLKETIIKNNseikdLTNQ 448
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1122-1226 9.48e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1122 LAATAGHVGVvEILLDNGADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 1201
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530376947 1202 LL---------NAGAEINSRTG--SKLGISPLMLAA 1226
Cdd:PTZ00322  167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1338-1405 1.05e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947 1338 LLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYL 1405
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1226-1315 1.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1226 AMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                          90
                  ....*....|....*
gi 530376947 1306 -----DKGADVNAPP 1315
Cdd:PTZ00322  169 rhsqcHFELGANAKP 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
417-486 1.65e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  417 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 486
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 1.67e-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: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 530376947   442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
780-887 1.73e-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: 49.63  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   780 SKQKSSSHLPANSQDVQGYITN--QSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLElAHADQLTKEKIEELNKTREE 857
Cdd:TIGR04523  236 KKQQEINEKTTEISNTQTQLNQlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKS 314
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 530376947   858 QIQKKQKILEELQKverEL--------QLKTQ-QQLKKQ 887
Cdd:TIGR04523  315 ELKNQEKKLEEIQN---QIsqnnkiisQLNEQiSQLKKE 350
Ank_4 pfam13637
Ankyrin repeats (many copies);
1152-1203 2.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 2.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947  1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 1203
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 2.90e-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: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 530376947   471 LTLAACGGHVELAALLIERGASLE 494
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1352-1381 2.91e-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: 42.19  E-value: 2.91e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 530376947   1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 3.03e-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: 42.19  E-value: 3.03e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 530376947    499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
326-520 3.13e-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: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  326 DVNAQSSTGNTALTYAC---AGGYVDVVKVLLESG-----------ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGA 391
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  392 GINTHSN------------EFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSG 457
Cdd:cd21882    98 DVSARATgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENS 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530376947  458 AQVnmpADSFESPLTLAACGGHVElaalliergaSLEEV-NDEGYTPLMEAAREGHEEMVALLL 520
Cdd:cd21882   174 AFV---CQMYNLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02859 PHA02859
ankyrin repeat protein; Provisional
314-428 3.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  314 VKIVKLLLAHKADVNAQSSTGNTAL--TYACAGGYV--DVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLL 386
Cdd:PHA02859   66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530376947  387 LENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQE 428
Cdd:PHA02859  145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
565-651 3.31e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  565 STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVC 644
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*..
gi 530376947  645 TVQFLIS 651
Cdd:PTZ00322  163 VVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
1118-1170 3.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 3.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530376947  1118 TPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLL 1170
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-531 3.52e-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: 3.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 530376947   499 EGYTPLMEAA-REGHEEMVALLLGQGANINAQTE 531
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
1285-1340 3.80e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 3.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376947  1285 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1340
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
804-886 4.07e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.28  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  804 PESIVEEAQGKLTELEQRIKEAIEKNAQlQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEE-LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQA 578

                  ...
gi 530376947  884 LKK 886
Cdd:PRK00409  579 IKE 581
PTZ00121 PTZ00121
MAEBL; Provisional
809-892 4.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  809 EEAQGKLTEL--EQRIKEAIEKNAQLQSLELAHADQLTKEkiEELNKTREEQIQKK----QKILEELQKVERElQLKTQQ 882
Cdd:PTZ00121 1616 EEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKaeedKKKAEEAKKAEED-EKKAAE 1692
                          90
                  ....*....|
gi 530376947  883 QLKKQYLEVK 892
Cdd:PTZ00121 1693 ALKKEAEEAK 1702
Ank_5 pfam13857
Ankyrin repeats (many copies);
386-438 5.47e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 5.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530376947   386 LLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-341 7.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530376947   303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYA 341
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
320-371 7.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530376947   320 LLAHK-ADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 371
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
1131-1261 8.53e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1131 VVEILLDNGADIEAQsERTKDTPLSLACSGGRQ-----EVVELLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 1202
Cdd:PHA02798   53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1203 LNAGAEINSRtgSKLGISPLMLAAMNGHTA---AVKLLLDMGSDINaqIETNRNTALTLACF 1261
Cdd:PHA02798  132 IENGADTTLL--DKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDIN--THNNKEKYDTLHCY 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1262-1393 8.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPV-----------PSSRDTALTIAADK 1330
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALddlsvlecavdSKNIDTIKAIIDNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1331 G------------------------------------------HY--------KFCELLIGRGAHIDVRNKKGNTPLWL- 1359
Cdd:PHA02876  235 SninkndlsllkairnedletslllydagfsvnsiddckntplHHasqapslsRLVPKLLERGADVNAKNIKGETPLYLm 314
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530376947 1360 AANGGHLDVVQLLVQAGADVDAADNRKITPLMAA 1393
Cdd:PHA02876  315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
348-522 9.98e-05

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: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  348 DVVKVLLEsgASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGIN----------THSNE---FKESALTLACYKGHL 414
Cdd:cd22194   124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  415 EMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaSLE 494
Cdd:cd22194   202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
                         170       180
                  ....*....|....*....|....*....
gi 530376947  495 EV-NDEGYTPLMEAAREGHEEMVALLLGQ 522
Cdd:cd22194   261 TIrNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1218-1246 1.07e-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: 40.70  E-value: 1.07e-04
                           10        20
                   ....*....|....*....|....*....
gi 530376947  1218 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1246
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-330 1.30e-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: 40.35  E-value: 1.30e-04
                           10        20
                   ....*....|....*....|....*....
gi 530376947   303 TPLMAAA-NGGHVKIVKLLLAHKADVNAQ 330
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-892 1.35e-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: 46.55  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   774 IRNKAASKQKSSSHLPANSQDVQGYI-----TNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSL--ELAHADQLTKE 846
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikDLTNQDSVKEL 454
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 530376947   847 KIEELNKTREEQIQKKQKILEELQKVERELQlKTQQQLKKQYLEVK 892
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELK 499
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1075-1204 1.39e-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: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1075 IDAQ-TESNHD--TALTLACAGGHEELVQTLLERGASIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 1137
Cdd:cd22194   130 INAEyTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947 1138 NGADIEAQSERTKDTPL---------SLACSGGRQEVVELLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 1204
Cdd:cd22194   210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
271-364 1.41e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  271 LCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90
                  ....*....|....
gi 530376947  351 KVLleSGASIEDHN 364
Cdd:PTZ00322  165 QLL--SRHSQCHFE 176
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1299-1452 1.45e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1299 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGAD 1378
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1379 VDAADNRKITPLMAAFRKGHVKVVRYLvkevNQFPSDS------ECMRYIATITDKEMLKKChLCMESIVQAKDRQAAEA 1452
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRIL----YHFASISdphaagDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATA 658
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
234-454 1.46e-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: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   234 DNRSLAEACSEGDVNAVRKLLIEgrsVNEHTEEGESLLcLACSAGYY----ELAQVLLAMH--------ANVEDRG-IKG 300
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLN---LSCRGAVGDTLL-HAISLEYVdaveAILLHLLAAFrksgplelANDQYTSeFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   301 DITPLMAAANGGHVKIVKLLLAHKADVNA-------QSSTGNTAL--------TYACAGGYvDVVKVLLESGASIEDHNE 365
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFyhgesplnAAACLGSP-SIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   366 NGHTplmeagsaghveVARLLLENgaginthsNEFKESALTLACykghlEMVRFLLEAGaDQEHKTDEMH--------TA 437
Cdd:TIGR00870  207 LGNT------------LLHLLVME--------NEFKAEYEELSC-----QMYNFALSLL-DKLRDSKELEvilnhqglTP 260
                          250
                   ....*....|....*..
gi 530376947   438 LMEACMDGHVEVARLLL 454
Cdd:TIGR00870  261 LKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
1252-1305 1.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530376947  1252 RNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1218-1246 1.81e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.81e-04
                            10        20
                    ....*....|....*....|....*....
gi 530376947   1218 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1246
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1073-1144 1.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1073 IDIDAQTEsNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:PHA03100  183 VPINIKDV-YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-604 1.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 530376947   559 DIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYA 604
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
570-669 2.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  570 EAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                          90       100
                  ....*....|....*....|
gi 530376947  650 ISKGANVNRttanNDHTVLS 669
Cdd:PHA02876  231 IDNRSNINK----NDLSLLK 246
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-528 2.41e-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: 2.41e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 530376947   499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
1093-1289 2.47e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1093 GGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLaCSGGRQEVVE---LL 1169
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYY-LSGTDDEVIErinLL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1170 LARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEinSRTGSKLGISPL--MLAAMNGHTAAVKLLLDMGSDiNAQ 1247
Cdd:PHA02946  127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGIS-PSK 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530376947 1248 IETNRNTALTLACFQ--GRTEVVSLLLDrKANVEHRAKTGLTPL 1289
Cdd:PHA02946  204 PDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
346-443 2.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  346 YVDVVKVLLESGASIE---DHNENGHT-PLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:PHA02884   45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 530376947  422 EAGADQEHKTDEMHTALMEACM 443
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1115-1145 2.91e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.91e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 530376947  1115 KGFTPLILAAT-AGHVGVVEILLDNGADIEAQ 1145
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1115-1144 3.16e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.16e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 530376947   1115 KGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
566-592 3.26e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.26e-04
                            10        20
                    ....*....|....*....|....*..
gi 530376947    566 TPLMEAAQEGHLELVKYLLAAGANVHA 592
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
566-594 3.27e-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: 39.19  E-value: 3.27e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 530376947   566 TPLMEAA-QEGHLELVKYLLAAGANVHATT 594
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-660 3.34e-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: 39.19  E-value: 3.34e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 530376947   630 GRTPLMKAA-RAGHVCTVQFLISKGANVNRTT 660
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
611-723 3.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  611 DVADVLLQAGADLEHESEGGRTPLMKAARAGHVCT-----VQFLISKGANVNRTTANNDHTVLSLACAG-GHLAVVELLL 684
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530376947  685 AHGADPTHRLKDGSTMLIEAAKGGH--TSVVCYLLDYPNNL 723
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
630-657 3.63e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.63e-04
                            10        20
                    ....*....|....*....|....*...
gi 530376947    630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
515-725 4.13e-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: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  515 MVALLlgqgaNINAQTEETQETALTLACCGGFLEVadfLIKAGADIE-LGCSTPLMEAAQEGHLELVKYLLAAGANVHAt 593
Cdd:cd22194    99 MKALL-----NINENTKEIVRILLAFAEENGILDR---FINAEYTEEaYEGQTALNIAIERRQGDIVKLLIAKGADVNA- 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  594 TATGdtaltyacenghtdvadVLLQAgadlEHESEG---GRTPLMKAAraghvCT-----VQFLISKGANVNRTTANNDH 665
Cdd:cd22194   170 HAKG-----------------VFFNP----KYKHEGfyfGETPLALAA-----CTnqpeiVQLLMEKESTDITSQDSRGN 223
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947  666 TVL-SLACAG----GHLAVV-----ELLLAHGAD--PTHRLKDGSTMLIEAAKGGHTSVVCYLL-----DYPNNLLS 725
Cdd:cd22194   224 TVLhALVTVAedskTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYILsreikEKPNRSLS 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
597-624 4.37e-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: 4.37e-04
                            10        20
                    ....*....|....*....|....*...
gi 530376947    597 GDTALTYACENGHTDVADVLLQAGADLE 624
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 4.55e-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: 4.55e-04
                            10        20
                    ....*....|....*....|....*....
gi 530376947    334 GNTALTYACAGGYVDVVKVLLESGASIED 362
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
303-329 5.93e-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: 38.34  E-value: 5.93e-04
                            10        20
                    ....*....|....*....|....*..
gi 530376947    303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
366-394 6.58e-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: 38.42  E-value: 6.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 530376947   366 NGHTPLMEA-GSAGHVEVARLLLENGAGIN 394
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1084-1231 7.05e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1084 DTALTLACAGGHEELVQTLLERGAS-----IEHRDKKGFTPLILAATAGHVGVVEILLDNGADIeaQSERTKDT------ 1152
Cdd:cd22192    52 ETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADV--VSPRATGTffrpgp 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1153 ---------PLSLACSGGRQEVVELLLARGANKEHRNVSDYTP---LSLAASGGYV-NIIKILLNAGAEINSRTGSKL-- 1217
Cdd:cd22192   130 knliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhiLVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVpn 209
                         170
                  ....*....|....*.
gi 530376947 1218 --GISPLMLAAMNGHT 1231
Cdd:cd22192   210 nqGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1087-1275 8.17e-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: 43.92  E-value: 8.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1087 LTLACAGGHEELVQTLLERGASIEHRDKkgftpLILAATAGHVGVVE----ILLDNGADI--------EAQSERTKD-TP 1153
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1154 LSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1219
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947  1220 SPLMLAAMNGHTAAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRTEVVSLLLDRK 1275
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
365-584 8.73e-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: 43.98  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  365 ENGHTPLMEAgsaghvevarlLLEngagINTHSNEFKESALTLACYKGHLEmvRFLleaGADQEHKTDEMHTALMEACMD 444
Cdd:cd22194    92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  445 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGAsleevndegyTPLMEAARE 510
Cdd:cd22194   152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKES----------TDITSQDSR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  511 GHEEMVALLlgqganINAQTEETQETALTlaccggflEVADFLIKAGADIELGCS------TPLMEAAQEGHLELVKYLL 584
Cdd:cd22194   222 GNTVLHALV------TVAEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYIL 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-893 9.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  808 VEEAQGKLTELEQRIKEAIEKNAQLQSLELahadqlTKEKIEELNKTREEQIQKKQKILEELQKVERElqLKTQQQLKKQ 887
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEG------SKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEE 294

                  ....*.
gi 530376947  888 YLEVKA 893
Cdd:PRK03918  295 YIKLSE 300
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1085-1136 9.64e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 9.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530376947 1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1136
Cdd:PTZ00322  117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-657 1.00e-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: 38.01  E-value: 1.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 530376947   630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
1097-1210 1.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1097 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL---DNGADIEAQSERTKdTPLSLACSGGRQ---EVVELLL 1170
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGF-TMLQVYLQSNHHidiEIIKLLL 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530376947 1171 ARGAN-KEHRNVSDYTPLSLAASGGY----VNIIKILLNAGAEIN 1210
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLHCYFKYNIdridADILKLFVDNGFIIN 213
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1120-1374 1.20e-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: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1120 LILAATAGHVGVVEILLDNGADIEAQS-ERTKDTPLSLACSGGR-QEVVELLLarganKEHRNVSDYTPLSLAASGGYVN 1197
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1198 ----IIKILLNAGAE------INSRTGSKL--GISPLMLAAMNGHTAAVKLLLDMGSDINAQietnrntaltlAC---FQ 1262
Cdd:TIGR00870   96 aveaILLHLLAAFRKsgplelANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAR-----------ACgdfFV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  1263 GRTEVVSLLLDRkanvehraktglTPLMEAASGGYAEVGRVLLDKGADVNAppvpssRDT-------ALTIAAD-KGHYK 1334
Cdd:TIGR00870  165 KSQGVDSFYHGE------------SPLNAAACLGSPSIVALLSEDPADILT------ADSlgntllhLLVMENEfKAEYE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947  1335 F----C-ELLIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1374
Cdd:TIGR00870  227 ElscqMyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1218-1247 1.25e-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: 37.65  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 530376947  1218 GISPLMLAA-MNGHTAAVKLLLDMGSDINAQ 1247
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
350-421 1.29e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376947  350 VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLL 421
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
805-881 1.32e-03

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: 39.06  E-value: 1.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947   805 ESIVEEAQgklTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEElnkTREEQIQKKQKILEELQKVERELQLKTQ 881
Cdd:TIGR02926   12 EELIEEAE---EERKQRIAEAREEARELLEEAEEEASKLGEEIIKE---AEEEIEKEAEKIREEGEKEIEAMKSKAK 82
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1352-1381 1.36e-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: 1.36e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 530376947  1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1142-1370 1.40e-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: 43.21  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1142 IEAQSERTKDTPLSL--ACSGGRQEVVELLlargANKEHRN-------VSDYTPLSLAASG-GYVNIIKILLNagaeINS 1211
Cdd:cd22194    36 AELAKEEQRDKKKRLkkVSEAAVEELGELL----KELKDLSrrrrktdVPDFLMHKLTASDtGKTCLMKALLN----INE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1212 RTGSklgISPLMLAAMNGHTAAVKLlldmgsdINAQIeTNRN----TALTLACFQGRTEVVSLLLDRKANVEHRAKT--- 1284
Cdd:cd22194   108 NTKE---IVRILLAFAEENGILDRF-------INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvff 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1285 -----------GLTPLMEAASGGYAEVGRVLLDKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------L 1338
Cdd:cd22194   177 npkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiL 251
                         250       260       270
                  ....*....|....*....|....*....|...
gi 530376947 1339 LIGRGAHID-VRNKKGNTPLWLAANGGHLDVVQ 1370
Cdd:cd22194   252 LKSENKNLEtIRNNEGLTPLQLAAKMGKAEILK 284
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
436-652 1.42e-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: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  436 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERgasleevndegytplmeaaREGH 512
Cdd:cd22193    31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  513 eeMVALLLGQGANINAQTeetqetaltlacCGGFLEVADflikAGADIELGcSTPLMEAAQEGHLELVKYLLA---AGAN 589
Cdd:cd22193    91 --IVALLVENGADVHAHA------------KGRFFQPKY----QGEGFYFG-ELPLSLAACTNQPDIVQYLLEnehQPAD 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530376947  590 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22193   152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
805-886 1.49e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIE---ELNKtREEQIQKKQKILEELQKVERELQLKTq 881
Cdd:COG2433   419 EEQVERLEAEVEELEAELEEKDERIERLER-ELSEARSEERREIRkdrEISR-LDREIERLERELEEERERIEELKRKL- 495

                  ....*
gi 530376947  882 QQLKK 886
Cdd:COG2433   496 ERLKE 500
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1085-1203 1.54e-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: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGF-------------TPLILAATAGHVGVVEILLDNGADIEAQSER--- 1148
Cdd:cd21882    75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdsl 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530376947 1149 -----------TKDTP--LSLACSggrqeVVELLLARGANKEH-------RNVSDYTPLSLAASGGYVNIIKILL 1203
Cdd:cd21882   155 gntvlhalvlqADNTPenSAFVCQ-----MYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530376947  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
Ank_5 pfam13857
Ankyrin repeats (many copies);
1135-1190 1.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376947  1135 LLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLA 1190
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
486-541 1.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947   486 LIERG-ASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETqETALTLA 541
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-886 1.68e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 1.68e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947    794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 869
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 530376947    870 QKV-ERELQLKTQQQLKK 886
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
PRK12704 PRK12704
phosphodiesterase; Provisional
809-884 1.78e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  809 EEAQGKLTELEQRIKEaieKNAQLQSLE--LAHADQLTKEKIEELNK------TREEQIQKKQKILEELQKVERELQLKT 880
Cdd:PRK12704   64 EEIHKLRNEFEKELRE---RRNELQKLEkrLLQKEENLDRKLELLEKreeeleKKEKELEQKQQELEKKEEELEELIEEQ 140

                  ....
gi 530376947  881 QQQL 884
Cdd:PRK12704  141 LQEL 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
435-462 1.78e-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: 1.78e-03
                            10        20
                    ....*....|....*....|....*...
gi 530376947    435 HTALMEACMDGHVEVARLLLDSGAQVNM 462
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-584 1.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530376947   536 TALTLACCGGFLEVADFLIKAGADI---ELGCSTPLMEAAQEGHLELVKYLL 584
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADInavDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
366-394 1.85e-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: 1.85e-03
                            10        20
                    ....*....|....*....|....*....
gi 530376947    366 NGHTPLMEAGSAGHVEVARLLLENGAGIN 394
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
398-527 1.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  398 NEFKESALtLACY---KGHLEMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02859   48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530376947  471 L--TLAACGGHVELAALLIERGASLEEVNDEG----YTPLMeaaREGHEEMVALLLGQGANIN 527
Cdd:PHA02859  127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
Ank_5 pfam13857
Ankyrin repeats (many copies);
1346-1390 2.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 2.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530376947  1346 IDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
805-892 2.15e-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: 42.70  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   805 ESIVEEAQGKLTELEQR---IKEAIEKNAQLQS--LELahadqltKEKIEELNKTREEQIQKKQKILEELQKVEREL-QL 878
Cdd:TIGR04523  186 QKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESqiSEL-------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLnQL 258
                           90
                   ....*....|....*....
gi 530376947   879 KTQQ-----QLKKQYLEVK 892
Cdd:TIGR04523  259 KDEQnkikkQLSEKQKELE 277
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
809-887 2.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  809 EEAQGKLTELEQRIKEAIEK----NAQLQSLElAHADQLTKEkIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ-- 882
Cdd:COG4372    76 EQLEEELEELNEQLQAAQAElaqaQEELESLQ-EEAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElk 153

                  ....*
gi 530376947  883 QLKKQ 887
Cdd:COG4372   154 ELEEQ 158
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
801-893 2.41e-03

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: 40.91  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   801 NQSPESIVEEAQGKLTELEQRIKE---AIEKNAQLQSlelahadQLTKE--KIEELNKTREEQIQKKQKILEELQKVERE 875
Cdd:pfam14988   28 VQECEEIERRRQELASRYTQQTAElqtQLLQKEKEQA-------SLKKElqALRPFAKLKESQEREIQDLEEEKEKVRAE 100
                           90
                   ....*....|....*...
gi 530376947   876 LQLKTQQqLKKQYLEVKA 893
Cdd:pfam14988  101 TAEKDRE-AHLQFLKEKA 117
HAUS4 pfam14735
HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. ...
812-892 2.42e-03

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: 41.09  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   812 QGKLTELEQRIKEAIEknaQLQSLELAHADQLTKekieeLNKTREEQIQKKQKILEELQKVERELQLKTQQQL---KKQY 888
Cdd:pfam14735   71 AAKLSRLPELLESEKR---RLESEKEKLRENLVL-----LQRQFAEYYQVLLQCLQLLQRLVLDHRLKHQSDLdrkKKEY 142

                   ....
gi 530376947   889 LEVK 892
Cdd:pfam14735  143 LEAK 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1082-1110 2.62e-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: 36.80  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 530376947   1082 NHDTALTLACAGGHEELVQTLLERGASIE 1110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1096-1238 2.75e-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: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1096 EELVQTLLERG-----------ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERT-------------KD 1151
Cdd:cd22194   110 KEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfGE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1152 TPLSLACSGGRQEVVELLL-----------ARGANKEHR--NVSDytplslaASGGYVNIIK-----ILLNAGAEINSRT 1213
Cdd:cd22194   190 TPLALAACTNQPEIVQLLMekestditsqdSRGNTVLHAlvTVAE-------DSKTQNDFVKrmydmILLKSENKNLETI 262
                         170       180
                  ....*....|....*....|....*
gi 530376947 1214 GSKLGISPLMLAAMNGHTAAVKLLL 1238
Cdd:cd22194   263 RNNEGLTPLQLAAKMGKAEILKYIL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1183-1210 2.91e-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: 36.41  E-value: 2.91e-03
                            10        20
                    ....*....|....*....|....*...
gi 530376947   1183 DYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1185-1320 2.95e-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: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1185 TPLSLAASGGYVNIIKILLNAGAEINSR-----------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNR- 1252
Cdd:cd21882    75 TALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSl 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1253 -NTALTLACFQGR---------TEVVSLLLDRKANVEHRAK-------TGLTPLMEAASGGYAEVGRVLLDKgaDVNAPP 1315
Cdd:cd21882   155 gNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR--EFSGPY 232

                  ....*
gi 530376947 1316 VPSSR 1320
Cdd:cd21882   233 QPLSR 237
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-892 2.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  808 VEEAQGKLTE----LEQRIKEAIEKNAQLQslELAHADQLTKEKIEELnKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:PRK03918  312 IEKRLSRLEEeingIEERIKELEEKEERLE--ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK 388

                  ....*....
gi 530376947  884 LKKQYLEVK 892
Cdd:PRK03918  389 LEKELEELE 397
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1164-1308 2.97e-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: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1164 EVVELLLA---------RGANKEHRNvSDY---TPLSLAASGGYVNIIKILLNAGAEINSRT------------GSKLGI 1219
Cdd:cd22194   111 EIVRILLAfaeengildRFINAEYTE-EAYegqTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykheGFYFGE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNT---ALTLAC--FQGRTEVVSLLLD------RKANVEH-RAKTGLT 1287
Cdd:cd22194   190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAedSKTQNDFVKRMYDmillksENKNLETiRNNEGLT 269
                         170       180
                  ....*....|....*....|....*.
gi 530376947 1288 PLMEAASGGYAEV-----GRVLLDKG 1308
Cdd:cd22194   270 PLQLAAKMGKAEIlkyilSREIKEKP 295
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
238-323 3.12e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGIKgdiTPLMAAANGGHVK 315
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENGFRE 162

                  ....*...
gi 530376947  316 IVKLLLAH 323
Cdd:PTZ00322  163 VVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
1202-1259 3.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 3.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  1202 LLNAGAeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLA 1259
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
380-538 3.84e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  380 VEVARLLLENGAGINTHSNEFKESALTLAC----YKGHLEMVRFLLEAGADQEHKTDEMHTALMeaCMdghvevarllLD 455
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY--CL----------LS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  456 SGAQVNMpadsfespltlaacgghvELAALLIERGASLEEVNDEGYTPLMEAAREGHE---EMVALLLGQGANINAQTEE 532
Cdd:PHA02798  119 NGYINNL------------------EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180

                  ....*.
gi 530376947  533 TQETAL 538
Cdd:PHA02798  181 EKYDTL 186
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
597-625 3.96e-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: 3.96e-03
                           10        20
                   ....*....|....*....|....*....
gi 530376947   597 GDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
808-893 3.97e-03

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: 41.97  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   808 VEEAQGKLTELEQRIKEaIEKNAQLQSLELAHADQltkeKIEELNKTREEQIQKKQKILEELQKVEREL-QLKTQQQLKK 886
Cdd:TIGR02168  283 IEELQKELYALANEISR-LEQQKQILRERLANLER----QLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLE 357

                   ....*..
gi 530376947   887 QYLEVKA 893
Cdd:TIGR02168  358 AELEELE 364
PHA02884 PHA02884
ankyrin repeat protein; Provisional
609-715 3.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  609 HTDVADVLLQAGADLEHE---SEGGRT-PLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLL 684
Cdd:PHA02884   45 YTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530376947  685 AHGADPTHRLKDGSTMlIEAAkgghtSVVCY 715
Cdd:PHA02884  125 SYGADINIQTNDMVTP-IELA-----LMICN 149
PHA02798 PHA02798
ankyrin-like protein; Provisional
1302-1411 4.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1302 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLIGRGAHIDVRNKKGNTPLW-LAANG--GHLDVVQLLV 1373
Cdd:PHA02798   55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530376947 1374 QAGADVDAADNRKITPLMAAFRKGH---VKVVRYLVK---EVNQ 1411
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1075-1113 4.59e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 4.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530376947  1075 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1113
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
775-890 4.78e-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: 40.95  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947   775 RNKAASKQKSSShlpANSQDVQGYItnQSPESIVEEAQGKLTELEQRI----KEAIEKNAQLQSLElahadqltkEKIEE 850
Cdd:pfam15905  165 RNKLEAKMKEVM---AKQEGMEGKL--QVTQKNLEHSKGKVAQLEEKLvsteKEKIEEKSETEKLL---------EYITE 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 530376947   851 LNKTREEQIQKKQKI--LEE-LQKVERELQ-LKTQQQLKKQYLE 890
Cdd:pfam15905  231 LSCVSEQVEKYKLDIaqLEElLKEKNDEIEsLKQSLEEKEQELS 274
PRK12704 PRK12704
phosphodiesterase; Provisional
805-886 5.00e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  805 ESIVEEAQ------GKLTELE-----QRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKtREEQIQKKQKILE------ 867
Cdd:PRK12704   41 KRILEEAKkeaeaiKKEALLEakeeiHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-KLELLEKREEELEkkekel 119
                          90       100
                  ....*....|....*....|....
gi 530376947  868 -----ELQKVERELQLKTQQQLKK 886
Cdd:PRK12704  120 eqkqqELEKKEEELEELIEEQLQE 143
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-329 5.48e-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: 5.48e-03
                           10        20
                   ....*....|....*....|....*..
gi 530376947   303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
1270-1327 6.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 6.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  1270 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1327
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1082-1114 6.32e-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: 35.73  E-value: 6.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 530376947  1082 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 1114
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
1131-1227 6.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1131 VVEILLDNGADIEAQ---SERTKDTPLSLACSGGRQEVVELLLARGAN-KEHRNVSDYTPLSLAASGGYVNIIKILLNAG 1206
Cdd:PHA02884   48 IIDAILKLGADPEAPfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADvNRYAEEAKITPLYISVLHGCLKCLEILLSYG 127
                          90       100
                  ....*....|....*....|.
gi 530376947 1207 AEINSRTGSKlgISPLMLAAM 1227
Cdd:PHA02884  128 ADINIQTNDM--VTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
403-426 6.79e-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: 35.64  E-value: 6.79e-03
                            10        20
                    ....*....|....*....|....
gi 530376947    403 SALTLACYKGHLEMVRFLLEAGAD 426
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGAD 27
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
808-893 7.26e-03

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: 39.91  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  808 VEEAQGKLTELEQRIKEAIE----KNAQLQSLELAHADQltKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:COG1579    98 IESLKRRISDLEDEILELMErieeLEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
                          90
                  ....*....|
gi 530376947  884 LKKQYLEVKA 893
Cdd:COG1579   176 LLALYERIRK 185
PHA02798 PHA02798
ankyrin-like protein; Provisional
1234-1425 7.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1234 VKLLLDMGSDINAqIETNRNTAL-----TLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGY---AEVGRVLL 1305
Cdd:PHA02798   54 VKLFINLGANVNG-LDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1306 DKGADvnappvpssrdtalTIAADKGHYKFCELLIGRGAHIDvrnkkgntplwlaangghLDVVQLLVQAGADVDAADNR 1385
Cdd:PHA02798  133 ENGAD--------------TTLLDKDGFTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNK 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530376947 1386 -KITPLMAAFRKG----HVKVVRYLV------KEVNQFpSDSECMRYIATI 1425
Cdd:PHA02798  181 eKYDTLHCYFKYNidriDADILKLFVdngfiiNKENKS-HKKKFMEYLNSL 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
417-685 8.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.49  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  417 VRFLLEAGAD--QEHKTDEMHTALMEAcMDGHVEVARLLLDSGAQVNMPAdSFESPLTLAACGGHV------ELAALLIE 488
Cdd:PHA02989   19 LEFLLRTGFDvnEEYRGNSILLLYLKR-KDVKIKIVKLLIDNGADVNYKG-YIETPLCAVLRNREItsnkikKIVKLLLK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  489 RGA--SLEEVNdeGYTPLMEAAREGH---EEMVALLLGQGANINAQTEETQETAL--TLACCGGFLEVADFLIKAGADI- 560
Cdd:PHA02989   97 FGAdiNLKTFN--GVSPIVCFIYNSNinnCDMLRFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLf 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  561 ---ELGCSTP----LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENG---HTDVADVL--LQAGADLEHESE 628
Cdd:PHA02989  175 ektSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLESFLDNNkilSKKEFKVLnfILKYIKINKKDK 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376947  629 GGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLLA 685
Cdd:PHA02989  255 KGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGD-TVLTYAIKHGNIDMLNRILQ 310
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-892 8.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947  808 VEEAQGKLTELEQRIKEAIEKNAQLQSLElahaDQLtkEKIEELNKTREEQIQKKQKILEELQKVEREL----------- 876
Cdd:PRK03918  517 LEELEKKAEEYEKLKEKLIKLKGEIKSLK----KEL--EKLEELKKKLAELEKKLDELEEELAELLKELeelgfesveel 590
                          90
                  ....*....|....*...
gi 530376947  877 --QLKTQQQLKKQYLEVK 892
Cdd:PRK03918  591 eeRLKELEPFYNEYLELK 608
Ank_5 pfam13857
Ankyrin repeats (many copies);
1168-1225 8.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 8.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530376947  1168 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 1225
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1281-1385 8.92e-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: 40.63  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376947 1281 RAKTGLTPLMEAA---SGGYAEVGRVLLDKGAD-------VNAPPV--PSSRDTALTIAADKGHYKFCELLIGRGAHIDV 1348
Cdd:cd21882    22 RGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDsgnpkelVNAPCTdeFYQGQTALHIAIENRNLNLVRLLVENGADVSA 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530376947 1349 RN-----KK--------GNTPLWLAANGGHLDVVQLLVQAGADVDAADNR 1385
Cdd:cd21882   102 RAtgrffRKspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
827-887 9.17e-03

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: 36.09  E-value: 9.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947  827 EKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 887
Cdd:cd22249    10 EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
PHA02795 PHA02795
ankyrin-like protein; Provisional
314-384 9.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.36  E-value: 9.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530376947  314 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA02795  201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARR 271
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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