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Conserved domains on  [gi|672077060|ref|XP_008768614|]
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ankyrin repeat domain 36 isoform X1 [Rattus norvegicus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12120816)

ankyrin repeat (ANK) domain-containing protein mediates specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-182 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAV 116
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--------NDGNTPLHLAA 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672077060  117 LENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1247-1544 1.35e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1247 RFPLKQDEKRENVEfmfpqkkpRLRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAI 1326
Cdd:TIGR02169  188 RLDLIIDEKRQQLE--------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1327 LQRLEVRLFKLKLTLRENSARIE--------QIQNHLLH-----------EGLLEDGTKKLIFQTQSLESTLEKQMNRNE 1387
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGEleaeiaslersIAEKERELEDAEERLAKLEAEIDKLLAEIE 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1388 ELRTELARFKKLFEETKKRLNNHED------RELGGPGESNISQFDMLIP----INMLKHELHNLKESWETTYYKYLHMI 1457
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEeledlrAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEELQRLS 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1458 VKLQFIEQELIAIKTEQKKcghllenqknLEKEVLDLKSWMREIETQArdQNNIKNLRDT-----NDAAMIHQIDLRIKN 1532
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINE----------LEEEKEDKALEIKKQEWKL--EQLAADLSKYeqelyDLKEEYDRVEKELSK 487

                          330
                   ....*....|..
gi 672077060  1533 MESQLAMLGAQQ 1544
Cdd:TIGR02169  488 LQRELAEAEAQA 499
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-182 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAV 116
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--------NDGNTPLHLAA 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672077060  117 LENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-138 3.64e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 3.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    37 IHKAASMGDIPQVQKLLEFGNiDVNITDRKKRTALHYACAHGQSEMVSLLLWYdCNIEARDreestalikNGYTPLILAV 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD---------NGRTALHYAA 69

                           90       100
                   ....*....|....*....|..
gi 672077060   117 LENKQEMVELLLRAAANINALD 138
Cdd:pfam12796   70 RSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 34-177 3.77e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   34 VKRIHKAASMG--------DIPQVQKLLEFGNiDVNITDRKKRTALHY--ACAHGQS-EMVSLLLWYDCNIEARDReest 102
Cdd:PHA03095    7 VDIIMEAALYDyllnasnvTVEEVRRLLAAGA-DVNFRGEYGKTPLHLylHYSSEKVkDIVRLLLEAGADVNAPER---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  103 alikNGYTPLILAVL-ENKQEMVELLLRAAANINALDNCKRSALiHA----VRIqSKNMISLLLQQGADPSLVDIYGATA 177
Cdd:PHA03095   82 ----CGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPL-HVylsgFNI-NPKVIRLLLRKGADVNALDLYGMTP 155
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1247-1544 1.35e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1247 RFPLKQDEKRENVEfmfpqkkpRLRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAI 1326
Cdd:TIGR02169  188 RLDLIIDEKRQQLE--------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1327 LQRLEVRLFKLKLTLRENSARIE--------QIQNHLLH-----------EGLLEDGTKKLIFQTQSLESTLEKQMNRNE 1387
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGEleaeiaslersIAEKERELEDAEERLAKLEAEIDKLLAEIE 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1388 ELRTELARFKKLFEETKKRLNNHED------RELGGPGESNISQFDMLIP----INMLKHELHNLKESWETTYYKYLHMI 1457
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEeledlrAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEELQRLS 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1458 VKLQFIEQELIAIKTEQKKcghllenqknLEKEVLDLKSWMREIETQArdQNNIKNLRDT-----NDAAMIHQIDLRIKN 1532
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINE----------LEEEKEDKALEIKKQEWKL--EQLAADLSKYeqelyDLKEEYDRVEKELSK 487

                          330
                   ....*....|..
gi 672077060  1533 MESQLAMLGAQQ 1544
Cdd:TIGR02169  488 LQRELAEAEAQA 499
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-185 1.54e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    35 KRIHKAASMGDIPQVQK-LLEFGNIDVNITDRKKRTALHYACAHGQS-EMVSLLLWYDCNI------------------- 93
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRdLEEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGavgdtllhaisleyvdave 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    94 ------EARDREESTALIKN---------GYTPLILAVLENKQEMVELLLRAAANINALDNCK--------------RSA 144
Cdd:TIGR00870   99 aillhlLAAFRKSGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 672077060   145 LIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFET 185
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-176 4.90e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   40 AASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLwyDCnieARD--REESTALIKNGYTPLILAVL 117
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EA---APElvNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672077060  118 ENKQEMVELLLRAAANINALDNC------KRSALIH--------AVRIQSKNMISLLLQQGADPSLVDIYGAT 176
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATgtffrpGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1270-1399 6.14e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 6.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1270 LRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSskkIQAILQRLEVRLFKLKLTLREnsARIE 1349
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE---LEAELEEKDERIERLERELSE--ARSE 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 672077060 1350 QIQNHLLHEGLledgtKKLIFQTQSLESTLEKQMNRNEELRTELARFKKL 1399
Cdd:COG2433   457 ERREIRKDREI-----SRLDREIERLERELEEERERIEELKRKLERLKEL 501
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-136 4.57e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 4.57e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 672077060    107 NGYTPLILAVLENKQEMVELLLRAAANINA 136
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1279-1515 6.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1279 GSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAILQRLEVRLFKLKLTLRENSARIEQIQNHLLHE 1358
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1359 GLLEDGTKKLIFQTQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDRElggpgesnisqfDMLIPINMLKHE 1438
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE------------EYLDELREIEKR 315

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672077060 1439 LHNLKEswettyykylhmivKLQFIEQELIAIKTEQKKCGHLLENQKNLEKEVLDLKSWMREIETQARDQNNIKNLR 1515
Cdd:PRK03918  316 LSRLEE--------------EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-182 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAV 116
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--------NDGNTPLHLAA 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672077060  117 LENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-182 1.27e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   30 GYTPvkrIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGY 109
Cdd:COG0666   120 GETP---LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD--------NDGE 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672077060  110 TPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-138 3.64e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 3.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    37 IHKAASMGDIPQVQKLLEFGNiDVNITDRKKRTALHYACAHGQSEMVSLLLWYdCNIEARDreestalikNGYTPLILAV 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD---------NGRTALHYAA 69

                           90       100
                   ....*....|....*....|..
gi 672077060   117 LENKQEMVELLLRAAANINALD 138
Cdd:pfam12796   70 RSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-183 2.22e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAV 116
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD--------DGGNTLLHAAA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672077060  117 LENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVF 183
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-171 3.22e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 3.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    71 LHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAVLENKQEMVELLLrAAANINALDNcKRSALIHAVR 150
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--------KNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAAR 70

                           90       100
                   ....*....|....*....|.
gi 672077060   151 IQSKNMISLLLQQGADPSLVD 171
Cdd:pfam12796   71 SGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 34-177 3.77e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   34 VKRIHKAASMG--------DIPQVQKLLEFGNiDVNITDRKKRTALHY--ACAHGQS-EMVSLLLWYDCNIEARDReest 102
Cdd:PHA03095    7 VDIIMEAALYDyllnasnvTVEEVRRLLAAGA-DVNFRGEYGKTPLHLylHYSSEKVkDIVRLLLEAGADVNAPER---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  103 alikNGYTPLILAVL-ENKQEMVELLLRAAANINALDNCKRSALiHA----VRIqSKNMISLLLQQGADPSLVDIYGATA 177
Cdd:PHA03095   82 ----CGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPL-HVylsgFNI-NPKVIRLLLRKGADVNALDLYGMTP 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-177 2.87e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKKRTALH-YACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPL--ILAVLENKQEMVE 125
Cdd:PHA03095   66 VRLLLEAG-ADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD--------KVGRTPLhvYLSGFNINPKVIR 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672077060  126 LLLRAAANINALDNCKRSALihAVRIQSKN----MISLLLQQGADPSLVDIYGATA 177
Cdd:PHA03095  137 LLLRKGADVNALDLYGMTPL--AVLLKSRNanveLLRLLIDAGADVYAVDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-182 5.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 5.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   41 ASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAH--GQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAV-- 116
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN--------SDGENLLHLYLes 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  117 LENKQEMVELLLRAAANINALDNCKR----------------SALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSY 180
Cdd:PHA03100  152 NKIDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231


                  ..
gi 672077060  181 AV 182
Cdd:PHA03100  232 AI 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-87 1.76e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 672077060    37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLL 87
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
52-115 5.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.59  E-value: 5.53e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672077060    52 LLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREestaliknGYTPLILA 115
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--------GLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-166 8.42e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 8.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   30 GYTPvkrIHKAAS--MGDIPQVQKLLEFGnIDVNITDRKKRTALHYA--CAHGQSEMVSLLLWYDCNIEARDREEStaLI 105
Cdd:PHA03100  106 GITP---LLYAISkkSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVNY--LL 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672077060  106 KN----------GYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGAD 166
Cdd:PHA03100  180 SYgvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-182 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWY--DCNIEARDReestalikngYTPLIL 114
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARgaDPDIPNTDK----------FSPLHL 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672077060  115 AVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYG-ATAQSYAV 182
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-145 1.31e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   30 GYTPvkrIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLwydcnieaRDREESTALIKNGY 109
Cdd:COG0666   186 GETP---LHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLL--------EAGADLNAKDKDGL 253

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 672077060  110 TPLILAVLENKQEMVELLLRAAANINALDNCKRSAL 145
Cdd:COG0666   254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-176 6.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 6.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWY---------------DCNIEARDREESTALIKNGYT--- 110
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgadvniialddlsvlECAVDSKNIDTIKAIIDNRSNink 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  111 ---PLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQS-KNMISLLLQQGADPSLVDIYGAT 176
Cdd:PHA02876  240 ndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGET 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-140 7.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 7.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAVLENKQEMVELLL 128
Cdd:PHA03100  175 VNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--------KYGDTPLHIAILNNNKEIFKLLL 245

                          90
                  ....*....|..
gi 672077060  129 RAAANINALDNC 140
Cdd:PHA03100  246 NNGPSIKTIIET 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-182 9.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 9.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   30 GYTPVKRihkAASMGDIPQVQKLLEFGNI-DVNITDrkKRTALHYACAHGQSEMVSLLLwyDCNIEARDreestALIKNG 108
Cdd:PHA02875   35 GISPIKL---AMKFRDSEAIKLLMKHGAIpDVKYPD--IESELHDAVEEGDVKAVEELL--DLGKFADD-----VFYKDG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672077060  109 YTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:PHA02875  103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-164 1.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAVLENKQEMVELLL 128
Cdd:PHA02874  107 IKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED--------DNGCYPIHIAIKHNFFDIIKLLL 177

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 672077060  129 RAAANINALDNCKRSALIHAVRIQSKNMISLLLQQG 164
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 29-182 2.08e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   29 TGYTPvkrIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNG 108
Cdd:PHA02878  167 KGNTA---LHYATENKDQRLTELLLSYG-ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD--------KCG 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672077060  109 YTPLILAVLENKQ-EMVELLLRAAANINALDNCKRSALIHaVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:PHA02878  235 NTPLHISVGYCKDyDILKLLLEHGVDVNAKSYILGLTALH-SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-183 2.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKKRTALHYACAHGQS-----EMVSLLLWYDCNIEARDreestaliKNGYTPLILAVLE--NKQ 121
Cdd:PHA03100   51 VKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPD--------NNGITPLLYAISKksNSY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  122 EMVELLLRAAANINALdNCKRSALIHA-------------------VRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 182
Cdd:PHA03100  122 SIVEYLLDNGANVNIK-NSDGENLLHLylesnkidlkilkllidkgVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAV 200


                  .
gi 672077060  183 F 183
Cdd:PHA03100  201 Y 201
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 40-173 2.32e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   40 AASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTAL--------------- 104
Cdd:PLN03192  532 VASTGNAALLEELLKAK-LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifril 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672077060  105 -----IKNGYTP---LILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIY 173
Cdd:PLN03192  611 yhfasISDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-181 3.43e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   30 GYTPvkrIHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHyACAHGQS---EMVSLLLWYDCNIEARDreestaliK 106
Cdd:PHA03095   83 GFTP---LHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFNinpKVIRLLLRKGADVNALD--------L 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  107 NGYTPLIlAVLENKQ---EMVELLLRAAANINALDNCKRSAL-IHAVRIQSKN-MISLLLQQGADPSLVDIYGATAQSYA 181
Cdd:PHA03095  151 YGMTPLA-VLLKSRNanvELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSM 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-184 4.09e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   52 LLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDreestaliKNGYTPLILAVLENKQEMVELLLRAA 131
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALAD--------ALGALLLLAAALAGDLLVALLLLAAG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 672077060  132 ANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFE 184
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 49-166 4.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKK-RTALHYACAHGQSEMVSLLLWYDCNIEARDREEStalikngyTPLILAVLENKQEMVELL 127
Cdd:PHA02878  150 TKLLLSYG-ADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNN--------SPLHHAVKHYNKPIVHIL 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 672077060  128 LRAAANINALDNCKRSALIHAV-RIQSKNMISLLLQQGAD 166
Cdd:PHA02878  221 LENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVD 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-182 7.98e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 7.98e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672077060   112 LILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQgADPSLVDiYGATAQSYAV 182
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAA 69
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-182 1.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   79 QSEMVSLLLWYDCNIEARDREEstaliknGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMIS 158
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHK-------GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                          90       100
                  ....*....|....*....|....
gi 672077060  159 LLLQQGADPSLVDIYGATAQSYAV 182
Cdd:PHA02878  219 ILLENGASTDARDKCGNTPLHISV 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-140 5.34e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   34 VKRIHKAASmGDIPQVQKLLEfGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREestaliknGYTPLI 113
Cdd:PTZ00322   84 VELCQLAAS-GDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD--------GKTPLE 153

                          90       100
                  ....*....|....*....|....*..
gi 672077060  114 LAVLENKQEMVELLLRAAANINALDNC 140
Cdd:PTZ00322  154 LAEENGFREVVQLLSRHSQCHFELGAN 180
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 1.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 672077060   108 GYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLL 161
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1247-1544 1.35e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1247 RFPLKQDEKRENVEfmfpqkkpRLRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAI 1326
Cdd:TIGR02169  188 RLDLIIDEKRQQLE--------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1327 LQRLEVRLFKLKLTLRENSARIE--------QIQNHLLH-----------EGLLEDGTKKLIFQTQSLESTLEKQMNRNE 1387
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGEleaeiaslersIAEKERELEDAEERLAKLEAEIDKLLAEIE 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1388 ELRTELARFKKLFEETKKRLNNHED------RELGGPGESNISQFDMLIP----INMLKHELHNLKESWETTYYKYLHMI 1457
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEeledlrAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEELQRLS 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1458 VKLQFIEQELIAIKTEQKKcghllenqknLEKEVLDLKSWMREIETQArdQNNIKNLRDT-----NDAAMIHQIDLRIKN 1532
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINE----------LEEEKEDKALEIKKQEWKL--EQLAADLSKYeqelyDLKEEYDRVEKELSK 487

                          330
                   ....*....|..
gi 672077060  1533 MESQLAMLGAQQ 1544
Cdd:TIGR02169  488 LQRELAEAEAQA 499
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-185 1.54e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    35 KRIHKAASMGDIPQVQK-LLEFGNIDVNITDRKKRTALHYACAHGQS-EMVSLLLWYDCNI------------------- 93
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRdLEEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGavgdtllhaisleyvdave 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060    94 ------EARDREESTALIKN---------GYTPLILAVLENKQEMVELLLRAAANINALDNCK--------------RSA 144
Cdd:TIGR00870   99 aillhlLAAFRKSGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 672077060   145 LIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFET 185
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-174 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMGDIPQVQKLLEFGNIdVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARdreestalIKNGYTPLILAV 116
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK--------CKNGFTPLHNAI 231

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672077060  117 LENKQeMVELLLRAAAnINALDNCKRSALIHAVRIQ-SKNMISLLLQQGADPSLVDIYG 174
Cdd:PHA02874  232 IHNRS-AIELLINNAS-INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKG 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 33-182 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   33 PVKRIHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKNGYTPL 112
Cdd:PHA02876   41 PFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIILDIKYASIILNKHKLDEA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  113 ILAVL-----------------------------ENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQ 163
Cdd:PHA02876  121 CIHILkeaisgndihydkinesieymklikeriqQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                         170
                  ....*....|....*....
gi 672077060  164 GADPSLVDIYGATAQSYAV 182
Cdd:PHA02876  201 GADVNIIALDDLSVLECAV 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 32-185 1.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   32 TPVKRIHKAASMGDIpqVQKLLEFGnIDVNITDRKKRTALHYACAHG-QSEMVSLLLWYDCNIEARDREESTALIKngyt 110
Cdd:PHA02876  275 TPLHHASQAPSLSRL--VPKLLERG-ADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQ---- 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672077060  111 pliLAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFET 185
Cdd:PHA02876  348 ---ASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT 419
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 2.12e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.12e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 672077060   107 NGYTPLILAVLE-NKQEMVELLLRAAANINALDN 139
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
68-128 2.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 2.22e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672077060    68 RTALHYACAHGQSEMVSLLLWYDCNIEARDReestalikNGYTPLILAVLENKQEMVELLL 128
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDG--------NGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-176 4.90e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   40 AASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLwyDCnieARD--REESTALIKNGYTPLILAVL 117
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EA---APElvNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672077060  118 ENKQEMVELLLRAAANINALDNC------KRSALIH--------AVRIQSKNMISLLLQQGADPSLVDIYGAT 176
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATgtffrpGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1265-1573 6.07e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 6.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1265 QKKPRLRREEEQHDGSVERTQRpEIRTVIAELKALEKDLRQLQGVQDQLAQTVQS-SKKIQAI---LQRLEVRLFKLKLT 1340
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASR-KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSlEQEIENVkseLKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1341 LRENSARIEQIQNHLLHEGL---------LEDGTKKLIFQTQSLESTLEKQMNRNEELRTELARFKKLFEETKKRlnnhe 1411
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSRIpeiqaelskLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----- 848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1412 drelggpgesnisqfdmlipINMLKHELHNLKeswettyykylhmiVKLQFIEQELiaiKTEQKKCGHLLENQKNLEKEV 1491
Cdd:TIGR02169  849 --------------------IKSIEKEIENLN--------------GKKEELEEEL---EELEAALRDLESRLGDLKKER 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1492 LDLKSWMREIETQARDQN---NIKNLRDTndaamihQIDLRIKNMESQLAMLGAQQHEggMSKYKPHHADEERCQNRSPT 1568
Cdd:TIGR02169  892 DELEAQLRELERKIEELEaqiEKKRKRLS-------ELKAKLEALEEELSEIEDPKGE--DEEIPEEELSLEDVQAELQR 962


                   ....*
gi 672077060  1569 MQERV 1573
Cdd:TIGR02169  963 VEEEI 967
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1270-1399 6.14e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 6.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1270 LRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSskkIQAILQRLEVRLFKLKLTLREnsARIE 1349
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE---LEAELEEKDERIERLERELSE--ARSE 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 672077060 1350 QIQNHLLHEGLledgtKKLIFQTQSLESTLEKQMNRNEELRTELARFKKL 1399
Cdd:COG2433   457 ERREIRKDREI-----SRLDREIERLERELEEERERIEELKRKLERLKEL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1269-1505 2.37e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1269 RLRREEEQHDGSVertqrpeirtVIAELKALEKDLRQLQgvqDQLAQTVQSSKKIQAILQRLEVRLFKLKLTLRENSARI 1348
Cdd:TIGR02168  217 ELKAELRELELAL----------LVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1349 EQIQNHLL-HEGLLEDGTKKLIFQTQSLES----------TLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDRelgg 1417
Cdd:TIGR02168  284 EELQKELYaLANEISRLEQQKQILRERLANlerqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAE---- 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1418 pgesnISQFDMLIPinMLKHELHNLKESWETTYYKYLHMIVKLQFIEQELIAIKTEQKkcgHLLENQKNLEKEVLDLKSW 1497
Cdd:TIGR02168  360 -----LEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKK 429


                   ....*...
gi 672077060  1498 MREIETQA 1505
Cdd:TIGR02168  430 LEEAELKE 437
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-98 2.40e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.40e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 672077060    68 RTALHYACAH-GQSEMVSLLLWYDCNIEARDR 98
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1283-1398 2.78e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1283 RTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAILQR---LEVRLFKLKLTLRENSARIEQIQNHL--Lh 1357
Cdd:COG3206   225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQlaeLEAELAELSARYTPNHPDVIALRAQIaaL- 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 672077060 1358 EGLLEDGTKKLIfqtQSLESTLEKQMNRNEELRTELARFKK 1398
Cdd:COG3206   304 RAQLQQEAQRIL---ASLEAELEALQAREASLQAQLAQLEA 341
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-166 3.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   37 IHKAASMG---DIpqVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTAL--------- 104
Cdd:PHA02876  345 LHQASTLDrnkDI--VITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhfalcgtnp 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  105 ---------------IKNGY--TPLILAVLEN-KQEMVELLLRAAANINALDNCKRSALIHAVRIQSknMISLLLQQGAD 166
Cdd:PHA02876  422 ymsvktlidrganvnSKNKDlsTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAE 499
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-136 4.57e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 4.57e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 672077060    107 NGYTPLILAVLENKQEMVELLLRAAANINA 136
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1285-1588 5.33e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1285 QRPEIRTVIAELKALEKDLRQLQgvqDQLAQTVQSSKKIQAILQRLEVRLFKLKLTLRENSARIEQIQNHLlheglledg 1364
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1365 tkklifqtqsleSTLEKQMnrnEELRTELARFKKLFeetKKRLNNHEDRELGGPGESNISQFDMLIPINMLkhelhnlke 1444
Cdd:COG4942    86 ------------AELEKEI---AELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRL--------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1445 swetTYYKYLhmivkLQFIEQELIAIKTEQKKcghLLENQKNLEKEVLDLKSWMREIETQARDQNNIKNLRdtndAAMIH 1524
Cdd:COG4942   139 ----QYLKYL-----APARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEERAALEALKAER----QKLLA 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1525 QIDLRIKNMESQLAMLG--AQQHEGGMSKYKPHHADEERCQNRSP--TMQERVAWPSQGE--QSWGNKPN 1588
Cdd:COG4942   203 RLEKELAELAAELAELQqeAEELEALIARLEAEAAAAAERTPAAGfaALKGKLPWPVSGRvvRRFGERDG 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-171 6.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060   49 VQKLLEFGnIDVNITDRKKRTALHYAcAHGQSEMVSLLLWYDCN---IEARDReestalikNGYTPLILAVLENKQEMVE 125
Cdd:PHA03095  205 VRELIRAG-CDPAATDMLGNTPLHSM-ATGSSCKRSLVLPLLIAgisINARNR--------YGQTPLHYAAVFNNPRACR 274

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 672077060  126 LLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVD 171
Cdd:PHA03095  275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1293-1506 7.94e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1293 IAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAILQRLEVRLFKLKltlrensARIEQIQNHLLHEGLLEdgtkklifQT 1372
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-------EELEKLEKLLQLLPLYQ--------EL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1373 QSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDrelggpgesnisqfdmlipinmLKHELHNLKESWETTYYK 1452
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAE----------------------LQEELEELLEQLSLATEE 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672077060 1453 YLH-MIVKLQFIEQELIAIKTEQKKcghLLENQKNLEKEVLDLKSWMREIETQAR 1506
Cdd:COG4717   193 ELQdLAEELEELQQRLAELEEELEE---AQEELEELEEELEQLENELEAAALEER 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
106-148 1.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 672077060   106 KNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHA 148
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 110-172 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672077060  110 TPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDI 172
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1288-1408 1.40e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1288 EIRTVIAELKALEKDLR-QLQGVQDQLAQTVQSSKKIQAILQRLEVRLFKLKLTLRENSARIEQIQN-----HLLHEgll 1361
Cdd:COG1579    21 RLEHRLKELPAELAELEdELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyeALQKE--- 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 672077060 1362 EDGTKKLIfqtQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLN 1408
Cdd:COG1579    98 IESLKRRI---SDLEDEILELMERIEELEEELAELEAELAELEAELE 141
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1189-1506 2.95e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1189 RSDERLTELKKSHCELLTRKLGKAEDKASGVQREQTEIKKpkswsqhkevawdELCDLRFPLKQDEKRENvefmfpqkkp 1268
Cdd:TIGR02169  212 RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE-------------ELEKLTEEISELEKRLE---------- 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1269 RLRREEEQHDGSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQsskKIQAILQRLEVRLFKLKLTLRENSARI 1348
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE---DAEERLAKLEAEIDKLLAEIEELEREI 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1349 EQIQnhlLHEGLLEDGTKKLIFQTQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHE---DRELGGPGESNISQ 1425
Cdd:TIGR02169  346 EEER---KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKrelDRLQEELQRLSEEL 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060  1426 FDMLIPINMLKHELHNLKESWETtyykylhMIVKLQFIEQELIAIK----TEQKKCGHLLENQKNLEKEVLDLKSWMREI 1501
Cdd:TIGR02169  423 ADLNAAIAGIEAKINELEEEKED-------KALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQRELAEA 495


                   ....*
gi 672077060  1502 ETQAR 1506
Cdd:TIGR02169  496 EAQAR 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1269-1413 3.34e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1269 RLRREEEQHDGSVERTQRpEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAIL--------QRLEVRLFKLKLT 1340
Cdd:COG4942    66 ALARRIRALEQELAALEA-ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYL 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672077060 1341 LRENSARIEQIQNHLlheGLLEDGTKKLIFQTQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDR 1413
Cdd:COG4942   145 APARREQAEELRADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1289-1413 4.40e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1289 IRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAILQRLEVRLFKLkLTLRENSARIEQIQNHLLHeglLEDGTKKL 1368
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELER---LDASSDDL 687

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 672077060 1369 ifqtQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDR 1413
Cdd:COG4913   688 ----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1279-1515 6.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1279 GSVERTQRPEIRTVIAELKALEKDLRQLQGVQDQLAQTVQSSKKIQAILQRLEVRLFKLKLTLRENSARIEQIQNHLLHE 1358
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672077060 1359 GLLEDGTKKLIFQTQSLESTLEKQMNRNEELRTELARFKKLFEETKKRLNNHEDRElggpgesnisqfDMLIPINMLKHE 1438
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE------------EYLDELREIEKR 315

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672077060 1439 LHNLKEswettyykylhmivKLQFIEQELIAIKTEQKKCGHLLENQKNLEKEVLDLKSWMREIETQARDQNNIKNLR 1515
Cdd:PRK03918  316 LSRLEE--------------EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
 
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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