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Conserved domains on  [gi|119621962|gb|EAX01557|]
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hCG1647671, isoform CRA_b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 561-846 1.77e-109

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


:

Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 339.27  E-value: 1.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  561 NHLMRDEIARLRLEIDTIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQ 640
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  641 KEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNSHI-------QILSQQLSKAESTS 713
Cdd:pfam14915  81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  714 SGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQSQNLLYQQQCNDA 793
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962  794 RKKADNQEKTIINIQVKCEDTVEKLQAECRK----LEENNKGLMKECTLLKERQCQY 846
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKqvllLEERNKELINECNHLKERLYQY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-263 1.10e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  37 KDLGMIHKAAIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQ 116
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 117 EEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPD 196
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 197 LTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKANK 263
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 268-893 1.00e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  268 LQNSNSEQDLEMTSEGEQERLEGCEssqpqvEEKMKKCRNKKMEVSRN-VHADDSDNYNDDVDELIHkiknrkpdnhQSP 346
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIQHLE------EEYKKEINDKEKQVSLLlIQITEKENKMKDLTFLLE----------ESR 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  347 GKENGEFDRLARKTSNEKSKVKSQIYFTDDLNDI------SGSSEKTSEDDELPYSDDENFMLLIKQSGMEckdfvSLSK 420
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQME-----ELNK 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  421 SKNATAACGRSIEDQKCYCERL-KVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKK---LCNLRFILQQqEEERI 496
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveLEELKKILAE-DEKLL 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  497 KAEELYEKDIEELKIMEEQYRTQTEVKKQSkltLKSLEVELkTVRSNSNQNFHTHERERDLWQENHLMRDeiARLRLEID 576
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKE---IHDLEIQL-TAIKTSEEHYLKEVEDLKTELEKEKLKN--IELTAHCD 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  577 TIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLtktitrysKELNVLMDENTMLNSELQKEKQSMSRLETEMEsy 656
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--------KQIENLEEKEMNLRDELESVREEFIQKGDEVK-- 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  657 rcrlaaalCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNShiqiLSQQLskaESTSSGLEtELHYEREALKEKTLHIEH 736
Cdd:pfam05483 566 --------CKLDKSEENARSIEYEVLKKEKQMKILENKCNN----LKKQI---ENKNKNIE-ELHQENKALKKKGSAENK 629

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  737 MQGVLSRTQRRLE-DIEHMYQNDQPILEKYvrkQQSVEDGlfQLQSQNLLyqQQCNDARKKADNQEKTIINIQVKCEDTV 815
Cdd:pfam05483 630 QLNAYEIKVNKLElELASAKQKFEEIIDNY---QKEIEDK--KISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKI 702

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  816 eklqAECRKLEENNKGLMKEctLLKERQCQ---YEKEKEEREVVRRQLQREVDDALNKQLLLEAMLEISSERRINLEDEA 892
Cdd:pfam05483 703 ----AEMVALMEKHKHQYDK--IIEERDSElglYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776


                  .
gi 119621962  893 Q 893
Cdd:pfam05483 777 K 777
 
Name Accession Description Interval E-value
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 561-846 1.77e-109

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 339.27  E-value: 1.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  561 NHLMRDEIARLRLEIDTIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQ 640
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  641 KEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNSHI-------QILSQQLSKAESTS 713
Cdd:pfam14915  81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  714 SGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQSQNLLYQQQCNDA 793
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962  794 RKKADNQEKTIINIQVKCEDTVEKLQAECRK----LEENNKGLMKECTLLKERQCQY 846
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKqvllLEERNKELINECNHLKERLYQY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-263 1.10e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  37 KDLGMIHKAAIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQ 116
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 117 EEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPD 196
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 197 LTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKANK 263
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-167 7.49e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   76 LLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHgANPNVRDmYGNTALHYAIDNENISMAR 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 119621962  156 KLLAYGADIEAR 167
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-202 7.46e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  59 LLRL-----NDLNDRDKKNRTAL--LLACAHGRPGVVADLVARKCQLNLTDSENRTAL-IKAVQCQeevCASI----LLE 126
Cdd:PHA03095 169 LLRLlidagADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSS---CKRSlvlpLLI 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119621962 127 HGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDN 202
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 440-720 7.22e-07

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: 53.14  E-value: 7.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   440 ERLKVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKKLCNLRFILQQQEEERIKAEELYEKDIEELKIMEEQYRTQ 519
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   520 TEVKKQSKLTLKSLEVELKTVRSNSNQNFHTHERERDlwqENHLMRDEIARLRLEIDTIKHQNQETEnkyfKDIEIIKEN 599
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRS---KVAQLELQIASLNNEIERLEARLERLE----DRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   600 NEDLEKTLKRNE-ETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLAAAlcdhDQRQSSKRDLQ 678
Cdd:TIGR02168  423 IEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARLDSLERLQ 498

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 119621962   679 LAFQS---TVNEWCHLQEDTNSHIQILSQQLSKAESTSSGLETEL 720
Cdd:TIGR02168  499 ENLEGfseGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-233 2.27e-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: 51.55  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 107 TALIKAVQCQEEVCASILLEHGA----NPNVRDMY-GNTALHYAIDNENISMARKLLAYGADIEA---------RSQD-- 170
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnl 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 171 ---GHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTAL-ILAarngstsvvyqlLQHNIDVFCQ 233
Cdd:cd22192  133 iyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhILV------------LQPNKTFACQ 187
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-166 3.64e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 119621962   137 YGNTALHYAIDNENISMARKLLAYGADIEA 166
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 605-905 8.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 8.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 605 KTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLafqst 684
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----- 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 685 vnewchLQEDTNSHIQILSQQLSKAESTSSGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEhmyqndqpilek 764
Cdd:COG1196  310 ------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------------ 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 765 yvRKQQSVEDGLFQLQSQNLLYQQQCNDARKKADNQEKTIINIqvkcEDTVEKLQAECRKLEENNKGLMKECTLLKERQC 844
Cdd:COG1196  372 --AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEALAELEEEEEEEEEALE 445

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119621962 845 QYEKEKEEREVVRRQLQREVDDALNKQLLLEAMLeissERRINLEDEAQSLKKKLGQMRSQ 905
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAAL----AELLEELAEAAARLLLLLEAEAD 502
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 268-893 1.00e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  268 LQNSNSEQDLEMTSEGEQERLEGCEssqpqvEEKMKKCRNKKMEVSRN-VHADDSDNYNDDVDELIHkiknrkpdnhQSP 346
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIQHLE------EEYKKEINDKEKQVSLLlIQITEKENKMKDLTFLLE----------ESR 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  347 GKENGEFDRLARKTSNEKSKVKSQIYFTDDLNDI------SGSSEKTSEDDELPYSDDENFMLLIKQSGMEckdfvSLSK 420
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQME-----ELNK 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  421 SKNATAACGRSIEDQKCYCERL-KVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKK---LCNLRFILQQqEEERI 496
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveLEELKKILAE-DEKLL 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  497 KAEELYEKDIEELKIMEEQYRTQTEVKKQSkltLKSLEVELkTVRSNSNQNFHTHERERDLWQENHLMRDeiARLRLEID 576
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKE---IHDLEIQL-TAIKTSEEHYLKEVEDLKTELEKEKLKN--IELTAHCD 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  577 TIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLtktitrysKELNVLMDENTMLNSELQKEKQSMSRLETEMEsy 656
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--------KQIENLEEKEMNLRDELESVREEFIQKGDEVK-- 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  657 rcrlaaalCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNShiqiLSQQLskaESTSSGLEtELHYEREALKEKTLHIEH 736
Cdd:pfam05483 566 --------CKLDKSEENARSIEYEVLKKEKQMKILENKCNN----LKKQI---ENKNKNIE-ELHQENKALKKKGSAENK 629

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  737 MQGVLSRTQRRLE-DIEHMYQNDQPILEKYvrkQQSVEDGlfQLQSQNLLyqQQCNDARKKADNQEKTIINIQVKCEDTV 815
Cdd:pfam05483 630 QLNAYEIKVNKLElELASAKQKFEEIIDNY---QKEIEDK--KISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKI 702

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  816 eklqAECRKLEENNKGLMKEctLLKERQCQ---YEKEKEEREVVRRQLQREVDDALNKQLLLEAMLEISSERRINLEDEA 892
Cdd:pfam05483 703 ----AEMVALMEKHKHQYDK--IIEERDSElglYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776


                  .
gi 119621962  893 Q 893
Cdd:pfam05483 777 K 777
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 75-269 8.78e-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: 43.15  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   75 ALLLACAHGRPGVVADLV--ARKCQLNLTDSENRTALIKAVQ---CQEevCASILLEHGANPNVrdmyGNTALHYA---- 145
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLeePKKLNINCPDRLGRSALFVAAIeneNLE--LTELLLNLSCRGAV----GDTLLHAIsley 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  146 IDNENISMARKLLAYGADI---EARSQD------GHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDN-------------- 202
Cdd:TIGR00870  94 VDAVEAILLHLLAAFRKSGpleLANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfy 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962  203 FGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVaskfqairgMISEYKANKRRKSLQ 269
Cdd:TIGR00870 174 HGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV---------MENEFKAEYEELSCQ 231
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 332-618 1.24e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.73  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   332 IHKIKNRKPDNHQSPGKENGEFDRLARKTSNEKSKVKSQIYFTDDLNDISGSSEKTSE-----------DDELPYSDDEN 400
Cdd:TIGR01612 1113 INKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEiekkienivtkIDKKKNIYDEI 1192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   401 FMLLIKQSGMEcKDFVSLSKSKNATAACGRSIedQKCYCERLKVKFQKMKNNISVLQKVLSETDKTKSQSehqnlqgkkk 480
Cdd:TIGR01612 1193 KKLLNEIAEIE-KDKTSLEEVKGINLSYGKNL--GKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS---------- 1259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   481 lcnlrfilqQQEEERIKAEELYEKDIEELKIMEEQYRTQTEVKKQSKLTLKSL-EVELKTVRSN---SNQNFHTHERERD 556
Cdd:TIGR01612 1260 ---------PEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIrEKSLKIIEDFseeSDINDIKKELQKN 1330

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   557 LWQ------ENHLMRDEIARLR--LEIDTIKHQNQETEnKYFKDIEiikENNEDLEKTLKrNEETLTKTI 618
Cdd:TIGR01612 1331 LLDaqkhnsDINLYLNEIANIYniLKLNKIKKIIDEVK-EYTKEIE---ENNKNIKDELD-KSEKLIKKI 1395
 
Name Accession Description Interval E-value
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 561-846 1.77e-109

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 339.27  E-value: 1.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  561 NHLMRDEIARLRLEIDTIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQ 640
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  641 KEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNSHI-------QILSQQLSKAESTS 713
Cdd:pfam14915  81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  714 SGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQSQNLLYQQQCNDA 793
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962  794 RKKADNQEKTIINIQVKCEDTVEKLQAECRK----LEENNKGLMKECTLLKERQCQY 846
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKqvllLEERNKELINECNHLKERLYQY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-263 1.10e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  37 KDLGMIHKAAIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQ 116
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 117 EEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPD 196
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 197 LTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKANK 263
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-272 5.41e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  37 KDLGMIHKAAIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQ 116
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 117 EEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPD 196
Cdd:COG0666   99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119621962 197 LTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKANKRRKSLQNSN 272
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-240 1.16e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  42 IHKAAIAGDVnKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCA 121
Cdd:COG0666   91 LHAAARNGDL-EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 122 SILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAID 201
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119621962 202 NFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTA 240
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-252 2.70e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 2.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  53 KVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHGANPN 132
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 133 VRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAA 212
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119621962 213 RNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAI 252
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-208 4.04e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 4.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  42 IHKAAIAGDVNKVmeSILLRLN-DLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVC 120
Cdd:COG0666  124 LHLAAYNGNLEIV--KLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 121 ASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAI 200
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                 ....*...
gi 119621962 201 DNFGRTAL 208
Cdd:COG0666  282 LLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-262 1.04e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  87 VVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEA 166
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 167 RSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVA 246
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                        170
                 ....*....|....*.
gi 119621962 247 SKFQAIRGMISEYKAN 262
Cdd:COG0666  163 NGNLEIVKLLLEAGAD 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-167 7.49e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   76 LLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHgANPNVRDmYGNTALHYAIDNENISMAR 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 119621962  156 KLLAYGADIEAR 167
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-234 9.28e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  142 LHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPdlTAIDNFGRTALILAARNGSTSVVY 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 119621962  222 QLLQHNIDVFCQD 234
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-202 7.46e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  59 LLRL-----NDLNDRDKKNRTAL--LLACAHGRPGVVADLVARKCQLNLTDSENRTAL-IKAVQCQeevCASI----LLE 126
Cdd:PHA03095 169 LLRLlidagADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSS---CKRSlvlpLLI 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119621962 127 HGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDN 202
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 52-262 7.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 7.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  52 NKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQ------CQEEVcASILL 125
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNikynltDVKEI-VKLLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 126 EHGANPNVRDMYGNTALHYAIDN--ENISMARKLLAYGADIEARSQDGHTSLLLAV--NRKKEQMVSFLLKKKPDLTAI- 200
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKn 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 201 ---------------DNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKAN 262
Cdd:PHA03100 174 rvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-228 4.93e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 4.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  31 GYRVRQK---DLGMIHKA----AIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAH--GRPGVVADLVARKCQLNLT 101
Cdd:PHA03100  58 GADINSStknNSTPLHYLsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 102 DSENRTALIKAVQCQEE----------------VCASI--LLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGAD 163
Cdd:PHA03100 138 NSDGENLLHLYLESNKIdlkilkllidkgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119621962 164 IEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDnfgRTALILAARNGSTSVVYQLLQHNI 228
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII---ETLLYFKDKDLNTITKIKMLKKSI 279
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-232 5.41e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.98  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  59 LLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHGANPNVRDMYG 138
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 139 NTALHYAIDNENISMARKLLAYgadieARSQDGHTS---LLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNG 215
Cdd:PLN03192 592 NTALWNAISAKHHKIFRILYHF-----ASISDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666

                        170
                 ....*....|....*..
gi 119621962 216 STSVVYQLLQHNIDVFC 232
Cdd:PLN03192 667 HVDMVRLLIMNGADVDK 683
PHA03095 PHA03095
ankyrin-like protein; Provisional
 53-247 2.79e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  53 KVMESILLRLN---DLNDRDKKNRTAL-LLACAHGRPGVVADLVARKCQLNLTDSENRTALikavqcqeEVCAS------ 122
Cdd:PHA03095  61 KVKDIVRLLLEagaDVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPL--------HVYLSgfninp 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 123 ----ILLEHGANPNVRDMYGNTALHYAIDNENISMA--RKLLAYGADIEARSQDGHTSL--LLAVNRKKEQMVSFLLKKK 194
Cdd:PHA03095 133 kvirLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAG 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119621962 195 PDLTAIDNFGRTALILAARNGS--TSVVYQLLQHNIDVFCQDISGWTAEDYAVAS 247
Cdd:PHA03095 213 CDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVF 267
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-220 8.31e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  51 VNKVMESILLRLN-DLNDRDKKNRTAL--LLACAHGRPGVVADLVARKCQLNLTDSENRTAL-IKAVQCQE-EVCASILL 125
Cdd:PHA03095 130 INPKVIRLLLRKGaDVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPrARIVRELI 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 126 EHGANPNVRDMYGNTALHYA--IDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNF 203
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMatGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                        170
                 ....*....|....*..
gi 119621962 204 GRTALILAARNGSTSVV 220
Cdd:PHA03095 290 GNTPLSLMVRNNNGRAV 306
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-201 1.16e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  109 LIKAVQCQEEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYgADIEARSqDGHTSLLLAVNRKKEQMVS 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 119621962  189 FLLKKKPDLTAID 201
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-135 1.23e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   42 IHKAAIAGDVNKVmESILLRLNDLNDRDKKNRTALLLACAHGRPGVVaDLVARKCQLNLTDsENRTALIKAVQCQEEVCA 121
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 119621962  122 SILLEHGANPNVRD 135
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-230 6.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 6.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  42 IHKAAIAGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGV-VADLVARKCQLNLTDSENRTALIKAVQCQEEVC 120
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 121 ASI-LLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQM-VSFLLKKKPDLT 198
Cdd:PHA02876 357 IVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119621962 199 AIDNFGRTALILAARNG-STSVVYQLLQHNIDV 230
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-228 1.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  64 DLNDRDK-KNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHGANPNVRDMYGNTAL 142
Cdd:PHA02878 159 DINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 143 HYAIDN-ENISMARKLLAYGADIEARSQ-DGHTSLLLAVnrKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVV 220
Cdd:PHA02878 239 HISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINI 316


                 ....*...
gi 119621962 221 YQLLQHNI 228
Cdd:PHA02878 317 GRILISNI 324
PHA03095 PHA03095
ankyrin-like protein; Provisional
 99-248 1.30e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  99 NLTDSENRTALIKAVQCQEEVCASI---LLEHGANPNVRDMYGNTALHYAIDNENISMA---RKLLAYGADIEARSQDGH 172
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNASNVTVEEvrrLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119621962 173 TSL-LLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTAL--ILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASK 248
Cdd:PHA03095  85 TPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-196 1.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  42 IHKAAIAGDVNKVMEsiLLRLNDLNDR--DKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQCQEEV 119
Cdd:PHA02875  72 LHDAVEEGDVKAVEE--LLDLGKFADDvfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119621962 120 CASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLL-LAVNRKKEQMVSFLLKKKPD 196
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-266 1.84e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  175 LLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQHnIDVFCQDiSGWTAEDYAVASKFQAIRG 254
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 119621962  255 MISEYKANKRRK 266
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-246 3.47e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  64 DLNDRDKKNRTALLlACAHG---RPGVVADLVARKCQLNLTDSENRT---ALIKAVQCQEEVCAsILLEHGANPNVRDMY 137
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNANVELLR-LLIDAGADVYAVDDR 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 138 GNTALHYAIDN--ENISMARKLLAYGADIEARSQDGHTSL--LLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAAR 213
Cdd:PHA03095 187 FRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119621962 214 NGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVA 246
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 138-231 8.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 8.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 138 GNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGST 217
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                         90
                 ....*....|....*.
gi 119621962 218 SVVYQLLQH--NIDVF 231
Cdd:PHA02875 182 AICKMLLDSgaNIDYF 197
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 119-192 9.42e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 9.42e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119621962 119 VCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLK 192
Cdd:PTZ00322  96 VGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-233 3.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  48 AGDVNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAVQ------------- 114
Cdd:PHA02874  11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 115 ----------CQEEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKE 184
Cdd:PHA02874  91 gvdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119621962 185 QMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQH--NIDVFCQ 233
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK 221
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-178 4.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 4.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119621962  124 LLEHG-ANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLA 178
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 113-239 6.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 113 VQCQEEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLK 192
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 193 KKPDL-----------------------------TAIDNFGRTALILAARNGSTS-VVYQLLQHNIDVFCQDISGWT 239
Cdd:PHA02876 233 NRSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-158 1.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119621962  105 NRTALIKAV-QCQEEVCASiLLEHGANPNVRDMYGNTALHYAIDNENISMARKLL 158
Cdd:pfam13637   1 ELTALHAAAaSGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 440-720 7.22e-07

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: 53.14  E-value: 7.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   440 ERLKVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKKLCNLRFILQQQEEERIKAEELYEKDIEELKIMEEQYRTQ 519
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   520 TEVKKQSKLTLKSLEVELKTVRSNSNQNFHTHERERDlwqENHLMRDEIARLRLEIDTIKHQNQETEnkyfKDIEIIKEN 599
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRS---KVAQLELQIASLNNEIERLEARLERLE----DRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   600 NEDLEKTLKRNE-ETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLAAAlcdhDQRQSSKRDLQ 678
Cdd:TIGR02168  423 IEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARLDSLERLQ 498

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 119621962   679 LAFQS---TVNEWCHLQEDTNSHIQILSQQLSKAESTSSGLETEL 720
Cdd:TIGR02168  499 ENLEGfseGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 508-751 1.11e-06

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: 52.75  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   508 ELKIMEEQYRTQTEVKKQSKLTLKSLEVELKTVRSNSNQnfhTHERERDLWQENHLMRDEIARLRLEIDTIKHQNQETEN 587
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   588 KYFKDIEIIKENNEDLEKT------LKRNEETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLA 661
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   662 AALCDHDQRQSSKRDLQL-----------------AFQSTVNEWCHLQEDTNSHIQILSQQLSKAESTSSGLETELHYER 724
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEdieslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                          250       260
                   ....*....|....*....|....*..
gi 119621962   725 EALKEKTLHIEHMQGVLSRTQRRLEDI 751
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNL 941
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-233 2.27e-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: 51.55  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 107 TALIKAVQCQEEVCASILLEHGA----NPNVRDMY-GNTALHYAIDNENISMARKLLAYGADIEA---------RSQD-- 170
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnl 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 171 ---GHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTAL-ILAarngstsvvyqlLQHNIDVFCQ 233
Cdd:cd22192  133 iyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhILV------------LQPNKTFACQ 187
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 154-231 3.45e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119621962 154 ARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVF 231
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-214 3.76e-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: 50.65  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 100 LTDSE------NRTALIKAV---QCQEEVCASILLEHG---------ANPNVRDMY--GNTALHYAIDNENISMARKLLA 159
Cdd:cd21882   15 LTDSAyqrgatGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelVNAPCTDEFyqGQTALHIAIENRNLNLVRLLVE 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119621962 160 YGADIEARSQD-------------GHTSLLLAVNRKKEQMVSFLLKKKPDLTAI---DNFGRT---ALILAARN 214
Cdd:cd21882   95 NGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqDSLGNTvlhALVLQADN 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-262 5.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  42 IHKAAIAGdvNKVMESILLRLN-DLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNltdsENRTALIKAVQCQEEVC 120
Cdd:PHA02876 182 IHYAAERG--NAKMVNLLLSYGaDVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLET 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 121 ASILLEHGANPNVRDMYGNTALHYAIDNENIS-MARKLLAYGADIEARSQDGHTSL-LLAVNRKKEQMVSFLLKKKPDLT 198
Cdd:PHA02876 256 SLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVN 335

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119621962 199 AIDNFGRTALILAAR-NGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAIRGMISEYKAN 262
Cdd:PHA02876 336 AADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-224 5.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119621962  171 GHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLL 224
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
138-191 1.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119621962  138 GNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLL 191
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 101-230 2.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 101 TDSENRTALIKAVQCQEEVCASILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVN 180
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119621962 181 RKKE-QMVSFLLKKKPDLTAIDNF-GRTALILAARngSTSVVYQLLQHNIDV 230
Cdd:PHA02878 244 YCKDyDILKLLLEHGVDVNAKSYIlGLTALHSSIK--SERKLKLLLEYGADI 293
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-244 2.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119621962  190 LLKKKP-DLTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYA 244
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-179 3.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  35 RQKDLGMIHKAAIAGDvNKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKAV- 113
Cdd:PHA02878 165 RHKGNTALHYATENKD-QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVg 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962 114 QCQEEVCASILLEHGANPNVRD-MYGNTALHYAIDNENISmaRKLLAYGADIEARSQDGHTSLLLAV 179
Cdd:PHA02878 244 YCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-166 3.64e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 119621962   137 YGNTALHYAIDNENISMARKLLAYGADIEA 166
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 623-899 3.80e-05

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: 47.74  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   623 KELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLAFQSTVNEWCHLqedtnshIQIL 702
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-------IAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   703 SQQLSKAESTSSGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQSQ 782
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   783 NLLYQQQCNDARKKADNQEKTIINIqvkcEDTVEKLQAECRKLEENNKGLMKECTLLKERQCQYEKEKEEREVVRRQLQR 862
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 119621962   863 EVDDALNKQLLLEAMLEISSERRINLEDEAQSLKKKL 899
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
Ank_5 pfam13857
Ankyrin repeats (many copies);
91-145 4.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962   91 LVARKCQLNLTDSENRTALIKAVQC--QEEVCasILLEHGANPNVRDMYGNTALHYA 145
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYgaLEIVR--VLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
61-112 4.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119621962   61 RLNDLNDRDKKNRTALLLACAHGRPGVVADLVARKCQLNLTDSENRTALIKA 112
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-166 7.17e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 7.17e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 119621962  137 YGNTALHYAIDNENISMARKLLAYGADIEA 166
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 605-905 8.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 8.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 605 KTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLAAALCDHDQRQSSKRDLQLafqst 684
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----- 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 685 vnewchLQEDTNSHIQILSQQLSKAESTSSGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEhmyqndqpilek 764
Cdd:COG1196  310 ------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------------ 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 765 yvRKQQSVEDGLFQLQSQNLLYQQQCNDARKKADNQEKTIINIqvkcEDTVEKLQAECRKLEENNKGLMKECTLLKERQC 844
Cdd:COG1196  372 --AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEALAELEEEEEEEEEALE 445

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119621962 845 QYEKEKEEREVVRRQLQREVDDALNKQLLLEAMLeissERRINLEDEAQSLKKKLGQMRSQ 905
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAAL----AELLEELAEAAARLLLLLEAEAD 502
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 268-893 1.00e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  268 LQNSNSEQDLEMTSEGEQERLEGCEssqpqvEEKMKKCRNKKMEVSRN-VHADDSDNYNDDVDELIHkiknrkpdnhQSP 346
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIQHLE------EEYKKEINDKEKQVSLLlIQITEKENKMKDLTFLLE----------ESR 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  347 GKENGEFDRLARKTSNEKSKVKSQIYFTDDLNDI------SGSSEKTSEDDELPYSDDENFMLLIKQSGMEckdfvSLSK 420
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQME-----ELNK 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  421 SKNATAACGRSIEDQKCYCERL-KVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKK---LCNLRFILQQqEEERI 496
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveLEELKKILAE-DEKLL 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  497 KAEELYEKDIEELKIMEEQYRTQTEVKKQSkltLKSLEVELkTVRSNSNQNFHTHERERDLWQENHLMRDeiARLRLEID 576
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKE---IHDLEIQL-TAIKTSEEHYLKEVEDLKTELEKEKLKN--IELTAHCD 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  577 TIKHQNQETENKYFKDIEIIKENNEDLEKTLKRNEETLtktitrysKELNVLMDENTMLNSELQKEKQSMSRLETEMEsy 656
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--------KQIENLEEKEMNLRDELESVREEFIQKGDEVK-- 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  657 rcrlaaalCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNShiqiLSQQLskaESTSSGLEtELHYEREALKEKTLHIEH 736
Cdd:pfam05483 566 --------CKLDKSEENARSIEYEVLKKEKQMKILENKCNN----LKKQI---ENKNKNIE-ELHQENKALKKKGSAENK 629

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  737 MQGVLSRTQRRLE-DIEHMYQNDQPILEKYvrkQQSVEDGlfQLQSQNLLyqQQCNDARKKADNQEKTIINIQVKCEDTV 815
Cdd:pfam05483 630 QLNAYEIKVNKLElELASAKQKFEEIIDNY---QKEIEDK--KISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKI 702

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  816 eklqAECRKLEENNKGLMKEctLLKERQCQ---YEKEKEEREVVRRQLQREVDDALNKQLLLEAMLEISSERRINLEDEA 892
Cdd:pfam05483 703 ----AEMVALMEKHKHQYDK--IIEERDSElglYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776


                  .
gi 119621962  893 Q 893
Cdd:pfam05483 777 K 777
PHA02946 PHA02946
ankyin-like protein; Provisional
 88-205 1.04e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  88 VADLVARKCQLNLTDSENRTALIKAVQCQEEVCASILLEHGANPNVRDMYGNTALHY--AIDNENISMARKLLAYGADIE 165
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119621962 166 ARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDNFGR 205
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGK 174
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-167 1.69e-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: 1.69e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119621962  137 YGNTALHYAIDNE-NISMARKLLAYGADIEAR 167
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNAR 32
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 95-208 1.96e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.18  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  95 KCQLNLTDSENRT-ALIKAVQCQEEVcasilLEHGANPNVRDMY--GNTALHYAIDNENISMARKLLAYGADIEARSQD- 170
Cdd:cd22196   53 KAMLNLHNGQNDTiSLLLDIAEKTGN-----LKEFVNAAYTDSYykGQTALHIAIERRNMHLVELLVQNGADVHARASGe 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119621962 171 -------------GHTSLLLAVNRKKEQMVSFLLK---KKPDLTAIDNFGRTAL 208
Cdd:cd22196  128 ffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVL 181
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 450-912 2.09e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   450 KNNISVLQKVLSETDKTKSQSEHQnLQGKKKLCNLRFILQQQEEERIKAEELYEKDIEELKIMEEQYRTQTEVKKQSKLT 529
Cdd:TIGR00618  221 KQVLEKELKHLREALQQTQQSHAY-LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   530 LKSLEVELKTVRSNSNQNFHTHERERDLWQENHLMRDEIARLRLEIDTIKHQNQETENKYFKDIEIIKENNEDLEKTLKR 609
Cdd:TIGR00618  300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   610 NEETLTKTITRYSKELNVLMDENTMLNSELQK----------EKQSMSRLETEMESYRCRLA----AALCDHDQRQSSKR 675
Cdd:TIGR00618  380 HIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrtsafrdLQGQLAHAKKQQELQQRYAElcaaAITCTAQCEKLEKI 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   676 DLQLAFQSTVNEWCHLQEdtnshIQILSQQLSKAESTSSGLETELHYEREALKEKTLHIE-HMQ--GVLSRTQRRLEDIE 752
Cdd:TIGR00618  460 HLQESAQSLKEREQQLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpARQdiDNPGPLTRRMQRGE 534

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   753 HMYQNDQPILEKYVRKQQSVEDGLFQLQSQNLLYQQQCNDARKKaDNQEKTIINIQVKCEDTVEKL---QAECRK----- 824
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLtekLSEAEDmlace 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   825 ----LEENNKGLMKECTLLKERQCQYEKEKEEREVVRRQLQREVDDALNKQLLLEAMLEISSERRINLEDEAQSLKKKLG 900
Cdd:TIGR00618  614 qhalLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693

                          490
                   ....*....|..
gi 119621962   901 QMRSQVCMKLSM 912
Cdd:TIGR00618  694 YWKEMLAQCQTL 705
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-92 2.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119621962   42 IHKAAIAGDVnKVMESILLRLNDLNDRDKKNRTALLLACAHGRPGVVADLV 92
Cdd:pfam13637   5 LHAAAASGHL-ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 190-252 2.72e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119621962 190 LLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASKFQAI 252
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-204 3.29e-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: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 122 SILLEHGANPNVRDMYGNTALHYAI--DNENIS--MARKLLAYGADIEA------RSQDGHTSLLLAVNRKKEQMVSFLL 191
Cdd:cd22192  153 RLLIEHGADIRAQDSLGNTVLHILVlqPNKTFAcqMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232

                         90       100
                 ....*....|....*....|....*..
gi 119621962 192 KKKP--------------DLTAIDNFG 204
Cdd:cd22192  233 QKRRhiqwtygpltstlyDLTEIDSWG 259
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 65-236 5.12e-04

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: 43.72  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  65 LNDRDKKNRTALLLACAHGRPGVVADLVARKCqlnlTDS--ENRTALIKAVQCQEEVCASILLEHGANPNVRD------- 135
Cdd:cd21882   35 LNLNDGVNEAIMLLLEAAPDSGNPKELVNAPC----TDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 136 ------MYGNTALHYAIDNENISMARKLLAYGADI---EARSQDGHT---SLLLAVNRKKE------QMVSFLL----KK 193
Cdd:cd21882  111 spgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTvlhALVLQADNTPEnsafvcQMYNLLLsygaHL 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119621962 194 KP--DLTAIDNF-GRTALILAARNGSTSVVYQLLQHNIDVFCQDIS 236
Cdd:cd21882  191 DPtqQLEEIPNHqGLTPLKLAAVEGKIVMFQHILQREFSGPYQPLS 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 488-759 5.53e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 488 LQQQEEERIKAEELYEKDIEELKIMEEQYRT----QTEVKKQSKLTLKSLEVELKTVRSNSNQNFHTHERERDLwqenhl 563
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEElrleLEELELELEEAQAEEYELLAELARLEQDIARLEERRREL------ 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 564 mRDEIARLRLEIDTIKHQNQETEnkyfKDIEIIKENNEDLEKTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQKEK 643
Cdd:COG1196  315 -EERLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 644 QSMSRLETEMESYRcRLAAALCDHDQRQSSKRDLQLAFQSTVNEWCHLQEDTNSHIQILSQQLSKAESTSSGLETELHYE 723
Cdd:COG1196  390 EALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 119621962 724 REALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQNDQ 759
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 67-214 6.02e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 43.69  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  67 DRDKKNRTALLLACAHGRPGVVADLVA--RKCQLNLTDSE------NRTALIKAV-QCQEEVCASI--LLEHGA------ 129
Cdd:cd22197    1 DPNRFDRDRLFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAVlNLQDGVNACImpLLEIDKdsgnpk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 130 ---NPNVRDMY--GNTALHYAIDNENISMARKLLAYGADIEARSQD-------------GHTSLLLAVNRKKEQMVSFLL 191
Cdd:cd22197   81 plvNAQCTDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLL 160

                        170       180
                 ....*....|....*....|....*....
gi 119621962 192 KKKPDLTAI---DNFGRT---ALILAARN 214
Cdd:cd22197  161 ENPHQPASLqaqDSLGNTvlhALVMIADN 189
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 75-269 8.78e-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: 43.15  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   75 ALLLACAHGRPGVVADLV--ARKCQLNLTDSENRTALIKAVQ---CQEevCASILLEHGANPNVrdmyGNTALHYA---- 145
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLeePKKLNINCPDRLGRSALFVAAIeneNLE--LTELLLNLSCRGAV----GDTLLHAIsley 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  146 IDNENISMARKLLAYGADI---EARSQD------GHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDN-------------- 202
Cdd:TIGR00870  94 VDAVEAILLHLLAAFRKSGpleLANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfy 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621962  203 FGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVaskfqairgMISEYKANKRRKSLQ 269
Cdd:TIGR00870 174 HGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV---------MENEFKAEYEELSCQ 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 698-899 1.24e-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: 42.74  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   698 HIQILSQQLSKAESTSSGLETELHYEREALKEKTLHIEHMQGVLSRTQRRLEDIEHMYQ---NDQPILEK----YVRKQQ 770
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaNEISRLEQqkqiLRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   771 SVEDGLFQLQSQNLLYQQQCNDARKKADNQEKTIINIQVKCEDTVEKLQAECRKLEEnnkglmkectlLKERQCQYEKEK 850
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE-----------LESRLEELEEQL 381

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 119621962   851 EEREVVRRQLQREVDDALNKQLLLEAMLEISSERRINLEDEAQSLKKKL 899
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 332-618 1.24e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.73  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   332 IHKIKNRKPDNHQSPGKENGEFDRLARKTSNEKSKVKSQIYFTDDLNDISGSSEKTSE-----------DDELPYSDDEN 400
Cdd:TIGR01612 1113 INKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEiekkienivtkIDKKKNIYDEI 1192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   401 FMLLIKQSGMEcKDFVSLSKSKNATAACGRSIedQKCYCERLKVKFQKMKNNISVLQKVLSETDKTKSQSehqnlqgkkk 480
Cdd:TIGR01612 1193 KKLLNEIAEIE-KDKTSLEEVKGINLSYGKNL--GKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS---------- 1259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   481 lcnlrfilqQQEEERIKAEELYEKDIEELKIMEEQYRTQTEVKKQSKLTLKSL-EVELKTVRSN---SNQNFHTHERERD 556
Cdd:TIGR01612 1260 ---------PEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIrEKSLKIIEDFseeSDINDIKKELQKN 1330

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   557 LWQ------ENHLMRDEIARLR--LEIDTIKHQNQETEnKYFKDIEiikENNEDLEKTLKrNEETLTKTI 618
Cdd:TIGR01612 1331 LLDaqkhnsDINLYLNEIANIYniLKLNKIKKIIDEVK-EYTKEIE---ENNKNIKDELD-KSEKLIKKI 1395
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
503-663 1.37e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 503 EKDIEELKIMEEQYRTQTEVKKQSKLTLKSLEVELKTVRsNSNQNFHTHERERDLWQENHLMRDEIARLRLEIDTIKHQN 582
Cdd:COG4717   77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 583 QETENKyFKDIEI----IKENNEDLEKTLKRNEETLTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRC 658
Cdd:COG4717  156 EELREL-EEELEEleaeLAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                 ....*
gi 119621962 659 RLAAA 663
Cdd:COG4717  235 ELEAA 239
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-246 1.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 119621962  204 GRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVA 246
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 186-280 1.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 186 MVSFLLKKKPDLTAIDNFGRTALILAARNGSTSVVYQLLQHNIDVFCQDISGWTAEDYAVASK-FQAIRGMI-SEYKANK 263
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnIDTIKAIIdNRSNINK 239

                         90
                 ....*....|....*..
gi 119621962 264 RRKSLQNSNSEQDLEMT 280
Cdd:PHA02876 240 NDLSLLKAIRNEDLETS 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
 130-202 1.77e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119621962 130 NPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKEQMVSFLLKKKPDLTAIDN 202
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 86-214 1.90e-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: 42.09  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  86 GVVADLVARKcqLNLTDSE------NRTALIKAV---QCQEEVCASILLEHG---------ANPNVRDMY--GNTALHYA 145
Cdd:cd22193    6 GFLQDLCRRR--KDLTDSEftesstGKTCLMKALlnlNPGTNDTIRILLDIAektdnlkrfINAEYTDEYyeGQTALHIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 146 IDNENISMARKLLAYGADIEARSQD--------------GHTSLLLAVNRKKEQMVSFLLK---KKPDLTAIDNFGRT-- 206
Cdd:cd22193   84 IERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTvl 163


                 ....*....
gi 119621962 207 -ALILAARN 214
Cdd:cd22193  164 hALVTVADN 172
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 447-752 2.56e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   447 QKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKKLCNLRFILQQQEEERIKAEELYEKDIEELKI--------MEEQYRT 518
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlanseLTEARTE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   519 QTEVKKQSKLTLKSLEVELKTVRSNSNQNFHTHERERDLWQENHLMRDEIARLRLEIDT-----------IKHQNQETEN 587
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmevqrlealLKAMKSECQG 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   588 KYFKDIEIIKENNEDLEKT------LKRNEETLTKTITRYS-KELNVLMDENTM--LNSELQKEKQSMSRLETEMESYRC 658
Cdd:pfam15921  445 QMERQMAAIQGKNESLEKVssltaqLESTKEMLRKVVEELTaKKMTLESSERTVsdLTASLQEKERAIEATNAEITKLRS 524

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   659 RLAAALCD------------HDQRQSSKRDLQLAFQSTVNEWchLQEDTNSHIQILSQQLSKA---ESTSSGLETELHYE 723
Cdd:pfam15921  525 RVDLKLQElqhlknegdhlrNVQTECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQHGRTAgamQVEKAQLEKEINDR 602

                          330       340
                   ....*....|....*....|....*....
gi 119621962   724 REALKEKTLHIEHMQGVLSRTQRRLEDIE 752
Cdd:pfam15921  603 RLELQEFKILKDKKDAKIRELEARVSDLE 631
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 480-899 3.65e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   480 KLCNLRFILQQQEEERIKAEELYEKDIEELKIMEEQYRTQTEvkkqskltLKSLEVELKTVRsnsnqnfhTHERERDLWQ 559
Cdd:TIGR00618  220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL--------LKQLRARIEELR--------AQEAVLEETQ 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   560 ENHLMRDEIARLRLEIDTIKHQNQETENKYFKdieiIKENNEDLEKTLKRNEETLTK--TITRYSKELNVLMDENTMLNS 637
Cdd:TIGR00618  284 ERINRARKAAPLAAHIKAVTQIEQQAQRIHTE----LQSKMRSRAKLLMKRAAHVKQqsSIEEQRRLLQTLHSQEIHIRD 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   638 ELQKEKQSMSRLETEMESYRCRLAAAlcdhDQRQSSKRDLQLAFQ--STVNEWCHLQEDTNSHIQILSQQLSKAESTSSg 715
Cdd:TIGR00618  360 AHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKelDILQREQATIDTRTSAFRDLQGQLAHAKKQQE- 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   716 LETELHYEREALKEKTLHIEHMQGV-LSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQSQNLLYQQQC---N 791
Cdd:TIGR00618  435 LQQRYAELCAAAITCTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCihpN 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   792 DARKKADNQEKTIINIQvKCEDTVEKLQAECRKLEENNKGLMKECTLLKERQCQYEKEKEEREVVRRQLQREVDDALNKQ 871
Cdd:TIGR00618  515 PARQDIDNPGPLTRRMQ-RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593

                          410       420
                   ....*....|....*....|....*...
gi 119621962   872 LLLEAMLEISSERRINLEDEAQSLKKKL 899
Cdd:TIGR00618  594 VRLQDLTEKLSEAEDMLACEQHALLRKL 621
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-234 5.94e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 5.94e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119621962  204 GRTALILAA-RNGSTSVVYQLLQHNIDVFCQD 234
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02917 PHA02917
ankyrin-like protein; Provisional
 122-200 6.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.37  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 122 SILLEHGANPNVRDMYGNTALHYAIDNENISMARKLLAYGADIEARSQDGHTSLLLAVNRKKE-QMVSFLLKKKPDLTAI 200
Cdd:PHA02917 436 NICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLLCHKPTLDCV 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 591-826 6.31e-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: 40.43  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   591 KDIEIIKENNEDLEKTLKRNE---ETLTKTITRYSKELNVLMDENTMLNS---ELQKE----KQSMSRLETEMESYRCRL 660
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEeelEELTAELQELEEKLEELRLEVSELEEeieELQKElyalANEISRLEQQKQILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   661 AAALCDHDQR-------QSSKRDLQLAFQSTVNEWCHLQEDTNS---HIQILSQQLSKAESTSSGLETELHYEREALKEK 730
Cdd:TIGR02168  312 ANLERQLEELeaqleelESKLDELAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962   731 TLHIEHMQGVLSRTQRRLEDIEHMYQNDQPILEKYVRKQQSVEDGLFQLQS----QNLLYQQQCNDAR----KKADNQEK 802
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeeleEELEELQEELERLeealEELREELE 471

                          250       260
                   ....*....|....*....|....
gi 119621962   803 TIINIQVKCEDTVEKLQAECRKLE 826
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLE 495
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 203-230 8.76e-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: 34.54  E-value: 8.76e-03
                          10        20
                  ....*....|....*....|....*...
gi 119621962  203 FGRTALILAARNGSTSVVYQLLQHNIDV 230
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 440-898 8.76e-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: 40.00  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  440 ERLKVKFQKMKNNISVLQKVLSETDKTKSQSEHQNLQGKKKLCNLRFILQQQEEERIKAEELyEKDIEELKIMEEQYRTQ 519
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL-ESQISELKKQNNQLKDN 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  520 TEVKKQS----KLTLKSLEVELKTVRSNSNQNFHT-HERERDLWQENHLMR---DEIARLRLEIDTIKHQNQETENKYFK 591
Cdd:TIGR04523 234 IEKKQQEinekTTEISNTQTQLNQLKDEQNKIKKQlSEKQKELEQNNKKIKeleKQLNQLKSEISDLNNQKEQDWNKELK 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  592 -DIEIIKENNEDLEKTLKRNEET---LTKTITRYSKELNVLMDENTMLNSELQKEKQSMSRLETEMESYRCRLaaalcdh 667
Cdd:TIGR04523 314 sELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI------- 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  668 dqrqsskrdlqlafqstvnewchlqEDTNSHIQILSQQLSKAESTSSGLETELHYEREALKEKTLHIEHMQGVLSRTQRR 747
Cdd:TIGR04523 387 -------------------------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962  748 LEDIEhmyqNDQPILEKYVRKQQSVEDglfQLQSQNLLYQQQCNDARKKADNQEKTIiniqVKCEDTVEKLQAECRKLEE 827
Cdd:TIGR04523 442 IKDLT----NQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQNLEQKQKEL----KSKEKELKKLNEEKKELEE 510

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119621962  828 NNKGLMKECTLLKERQCQYEKEKEEREVVRRQLQREV--DDALNKQLLLEAMLEISSERRINLEDEAQSLKKK 898
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 138-217 9.72e-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: 39.74  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621962 138 GNTALHYAIDNENISMARKLLAYGADIEARSQD--------------GHTSLLLAVNRKKEQMVSFLLKKKPD-LTAIDN 202
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                         90
                 ....*....|....*...
gi 119621962 203 FGRT---ALILAARNGST 217
Cdd:cd22194  221 RGNTvlhALVTVAEDSKT 238
 
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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