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Conserved domains on  [gi|511836369|ref|XP_004742773|]
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ankyrin repeat domain-containing protein 12 isoform X1 [Mustela putorius furo]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

PubMed:  15152081

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
PTZ00121 super family cl31754
MAEBL; Provisional
 720-1176 7.68e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  720 KKSKLEKNIKEDKSTKEKHVSKERNFKEEREKIKKESEKSFREEKTKDLKEERENIPIDKETEcsslgTNASEESTGLHS 799
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-----KKAAAAKKKADE 1422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  800 MEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEKEKKTKHEHKSEKDKFDLSDCVDRIKEKDRLYSHHSERC 879
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  880 HKEGEKIKNITTVKKTDDREKSREKidRKHDKEKPEKERHLAENKEKHLIEKKNKQADNSDytkseksknkeKDREVDKK 959
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-----------EKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  960 EKS--------------RDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRY 1025
Cdd:PTZ00121 1570 KKAeedknmalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369 1026 KERDKHKDKIQLNSL-LKVKSEADKPKLKSS-PASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQK 1103
Cdd:PTZ00121 1650 EELKKAEEENKIKAAeEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511836369 1104 EKERLRNRNCLELKVKDKEKTKHslaESKNKELTRSKSSELTDAYTKEKQSKDVVSNRSQSVDAKNITNLGKS 1176
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-277 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 268
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 511836369   269 LLLRHGGNP 277
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-290 5.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  254 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 290
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 185-256 1.13e-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: 50.40  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  185 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 250
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 511836369  251 DDTPLH 256
Cdd:cd22192   169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 218-245 2.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 2.85e-05
                            10        20
                    ....*....|....*....|....*...
gi 511836369    218 GWTPLHEACNVGYYDVAKILIAAGADVN 245
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00121 PTZ00121
MAEBL; Provisional
 720-1176 7.68e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  720 KKSKLEKNIKEDKSTKEKHVSKERNFKEEREKIKKESEKSFREEKTKDLKEERENIPIDKETEcsslgTNASEESTGLHS 799
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-----KKAAAAKKKADE 1422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  800 MEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEKEKKTKHEHKSEKDKFDLSDCVDRIKEKDRLYSHHSERC 879
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  880 HKEGEKIKNITTVKKTDDREKSREKidRKHDKEKPEKERHLAENKEKHLIEKKNKQADNSDytkseksknkeKDREVDKK 959
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-----------EKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  960 EKS--------------RDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRY 1025
Cdd:PTZ00121 1570 KKAeedknmalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369 1026 KERDKHKDKIQLNSL-LKVKSEADKPKLKSS-PASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQK 1103
Cdd:PTZ00121 1650 EELKKAEEENKIKAAeEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511836369 1104 EKERLRNRNCLELKVKDKEKTKHslaESKNKELTRSKSSELTDAYTKEKQSKDVVSNRSQSVDAKNITNLGKS 1176
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 792-1156 2.77e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   792 EESTGLHSMEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEkekktkhehksEKDKFDLSDCVDRIKEKDRL 871
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-----------ALEYYQLKEKLELEEEYLLY 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   872 YSHHSERCHKEGEKIKNITTVKKTDdrEKSREKIDRKHDKEKPEKERHLAENKEKHLIEKKNKQADnsdyTKSEKSKNKE 951
Cdd:pfam02463  229 LDYLKLNEERIDLLQELLRDEQEEI--ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA----KEEEELKSEL 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   952 KDREVDKKEKSRDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKH 1031
Cdd:pfam02463  303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  1032 KDKIQLNSLLKVKSEADKPKLKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNR 1111
Cdd:pfam02463  383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 511836369  1112 NCLELKVKDKEKTKHSLAESKNKELTRSKSSELTDAYTKEKQSKD 1156
Cdd:pfam02463  463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-291 1.83e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  174 QKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 511836369  254 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-311 8.70e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 8.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 511836369  258 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDE 311
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-291 7.52e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  175 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511836369  255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-277 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 268
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 511836369   269 LLLRHGGNP 277
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-286 1.33e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          90       100
                  ....*....|....*....|....*....
gi 511836369  258 SASSGHRDIVKLLLRHGGNPFQANKHGER 286
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-290 5.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  254 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 290
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-247 3.50e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 3.50e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   178 VNKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 247
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 177-291 7.14e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 7.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 511836369  257 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-276 2.46e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  120 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPNHPSQTTPAQKKNPSS-----SSRQKDkVNKRNERGETPLHM 191
Cdd:PHA03100   69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  192 AAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03100  148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                         170       180
                  ....*....|....*....|...
gi 511836369  254 PLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 147-276 2.82e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.02  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  147 DNSPDSTPNHPSQTTPAQKKNPSSSSRQKDkVNKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:PHA02876  270 DDCKNTPLHHASQAPSLSRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 511836369  226 CNVGYY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876  349 STLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 190-284 4.66e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 71.47  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  190 HMAAiRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKL 269
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|....*
gi 511836369  270 LLRHGGNPFQANKHG 284
Cdd:PTZ00322  167 LSRHSQCHFELGANA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-291 1.02e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  175 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511836369  255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 178-291 2.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 511836369  258 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874  261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 178-274 5.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNE-RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90
                  ....*....|....*....
gi 511836369  257 DSASS-GHRDIVKLLLRHG 274
Cdd:PHA02878  240 ISVGYcKDYDILKLLLEHG 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 186-273 5.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  186 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90
                  ....*....|.
gi 511836369  263 HRDIVKLLLRH 273
Cdd:PHA02875  147 DIKGIELLIDH 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 146-291 6.13e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  146 RDNSPDSTPNHPSQTTPAQKKNPSSSSRQKdKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  226 cnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02878  242 --VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-287 9.81e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 9.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 250
Cdd:PHA03095  110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511836369  251 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 287
Cdd:PHA03095  187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 197-276 1.61e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  197 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 272
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                  ....
gi 511836369  273 HGGN 276
Cdd:PHA03095  106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
187-238 1.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 511836369   187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 238
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
218-271 2.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 511836369   218 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 271
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 197-291 2.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  197 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 275
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90
                  ....*....|....*.
gi 511836369  276 NPFQANKHGERPVDVA 291
Cdd:PHA02878  226 STDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 177-246 2.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 2.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
178-225 2.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 511836369   178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
177-255 2.98e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 2.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511836369  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 255
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 187-276 3.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 265
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                          90
                  ....*....|.
gi 511836369  266 IVKLLLRHGGN 276
Cdd:PHA02875  217 IVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 189-252 5.09e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 5.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511836369  189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-275 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  118 KKSTPVSILF--GYplsERKQMALLMQMTARDNSPDS---TPNHPSQTTPAQKKNPSSSSRQKDKVNKRNERGETPLHMA 192
Cdd:PHA02876  306 KGETPLYLMAknGY---DTENIRTLIMLGADVNAADRlyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  193 AIRGDV----------------------------------KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKIL 237
Cdd:PHA02876  383 AVRNNVviintlldygadiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEML 462

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 511836369  238 IAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 275
Cdd:PHA02876  463 LDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 184-285 1.14e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  184 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 246
Cdd:PLN03192  557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 511836369  247 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 285
Cdd:PLN03192  637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 178-284 2.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  178 VNKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 246
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511836369  247 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 284
Cdd:PHA02859  119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
237-291 2.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 511836369   237 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 143-272 4.80e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  143 MTARDNSPDSTPNHPSQTTPAQKKNPSSSSRQKDKVNKRNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWT 220
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 511836369  221 PLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLR 272
Cdd:PHA03095  260 PLHYA---AVFNnprACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-215 5.39e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 5.39e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 511836369   184 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 215
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 183-291 7.12e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  183 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100
                  ....*....|....*....|....*....
gi 511836369  263 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 291
Cdd:PHA02875  180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 185-256 1.13e-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: 50.40  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  185 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 250
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 511836369  251 DDTPLH 256
Cdd:cd22192   169 GNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 234-291 1.21e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511836369  234 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 187-276 1.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSAS- 260
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISk 116

                          90
                  ....*....|....*..
gi 511836369  261 -SGHRDIVKLLLRHGGN 276
Cdd:PHA03100  117 kSNSYSIVEYLLDNGAN 133
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 218-245 1.40e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.40e-05
                           10        20
                   ....*....|....*....|....*....
gi 511836369   218 GWTPLHEAC-NVGYYDVAKILIAAGADVN 245
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 201-288 2.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  201 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 280
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                  ....*...
gi 511836369  281 NKHGERPV 288
Cdd:PHA02874  187 DNNGESPL 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 218-245 2.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 2.85e-05
                            10        20
                    ....*....|....*....|....*...
gi 511836369    218 GWTPLHEACNVGYYDVAKILIAAGADVN 245
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-276 3.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  165 KKNPSSSSRQKDKVNKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 239
Cdd:PHA02876  126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511836369  240 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876  200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-256 4.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 4.07e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 511836369   209 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 250-277 4.30e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 4.30e-05
                            10        20
                    ....*....|....*....|....*...
gi 511836369    250 DDDTPLHDSASSGHRDIVKLLLRHGGNP 277
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-213 4.47e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 4.47e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 511836369    184 RGETPLHMAAIRGDVKQVKELISLGANVNV 213
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00121 PTZ00121
MAEBL; Provisional
 720-1176 7.68e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  720 KKSKLEKNIKEDKSTKEKHVSKERNFKEEREKIKKESEKSFREEKTKDLKEERENIPIDKETEcsslgTNASEESTGLHS 799
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-----KKAAAAKKKADE 1422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  800 MEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEKEKKTKHEHKSEKDKFDLSDCVDRIKEKDRLYSHHSERC 879
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  880 HKEGEKIKNITTVKKTDDREKSREKidRKHDKEKPEKERHLAENKEKHLIEKKNKQADNSDytkseksknkeKDREVDKK 959
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-----------EKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  960 EKS--------------RDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRY 1025
Cdd:PTZ00121 1570 KKAeedknmalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369 1026 KERDKHKDKIQLNSL-LKVKSEADKPKLKSS-PASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQK 1103
Cdd:PTZ00121 1650 EELKKAEEENKIKAAeEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511836369 1104 EKERLRNRNCLELKVKDKEKTKHslaESKNKELTRSKSSELTDAYTKEKQSKDVVSNRSQSVDAKNITNLGKS 1176
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 250-282 2.00e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 2.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 511836369   250 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 282
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 192-270 2.66e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511836369  192 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 270
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-215 2.88e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 2.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 511836369   176 DKVNKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 215
Cdd:pfam12796   51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
 198-284 3.51e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  198 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 266
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                          90
                  ....*....|....*...
gi 511836369  267 VKLLLRHGGNPFQANKHG 284
Cdd:PHA02798  128 LLFMIENGADTTLLDKDG 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-213 4.03e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 4.03e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 511836369   184 RGETPLHMAAIRGDVKQVKELISLGANVNV 213
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 218-246 4.32e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.32e-04
                           10        20
                   ....*....|....*....|....*....
gi 511836369   218 GWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00121 PTZ00121
MAEBL; Provisional
 808-1066 9.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  808 KQEKHIKENKEKSERRFQTKEKDVEKTERKNSEKEKKTKHEHKSEKDKFDLSdcvdRIKEKDRLYSHHSERCHKEGEKIK 887
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA----RMAHFARRQAAIKAEEARKADELK 1284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  888 NITTVKKTDDREKSREKIDRKHDKEKPEKERHLAENKEKHLIEKKNKQADNSDYTKSEKSKNKEKDREVDKKEKSRDKEG 967
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  968 VNITNTKHIQEEKKSSIADSSKAQH-EKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKI-QLNSLLKVKS 1045
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAK 1444

                         250       260
                  ....*....|....*....|.
gi 511836369 1046 EADKPKLKSSPASKDTRPKEK 1066
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKK 1465
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-205 2.41e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 2.41e-03
                           10        20
                   ....*....|....*....|....*...
gi 511836369   178 VNKRNERGETPLHMAAIRGDVKQVKELI 205
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 792-1156 2.77e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   792 EESTGLHSMEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEkekktkhehksEKDKFDLSDCVDRIKEKDRL 871
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-----------ALEYYQLKEKLELEEEYLLY 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   872 YSHHSERCHKEGEKIKNITTVKKTDdrEKSREKIDRKHDKEKPEKERHLAENKEKHLIEKKNKQADnsdyTKSEKSKNKE 951
Cdd:pfam02463  229 LDYLKLNEERIDLLQELLRDEQEEI--ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA----KEEEELKSEL 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   952 KDREVDKKEKSRDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKH 1031
Cdd:pfam02463  303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  1032 KDKIQLNSLLKVKSEADKPKLKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNR 1111
Cdd:pfam02463  383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 511836369  1112 NCLELKVKDKEKTKHSLAESKNKELTRSKSSELTDAYTKEKQSKD 1156
Cdd:pfam02463  463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 185-291 3.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369  185 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 263
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                          90       100
                  ....*....|....*....|....*...
gi 511836369  264 RDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLA 142
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 717-1047 4.26e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   717 LTEKKSKLEKNIKEDKSTKEKHVSKERNFKEEREKIKKESEKSFREEKTKDLKEEREN--IPIDKETECSSLGTNASEES 794
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEylLYLDYLKLNEERIDLLQELL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   795 TglhSMEKEIEMEKQEKHIKENKEKSERRFQTKEKDVEKTERKNSEKEKKTKHEHKSEKDKFDLsdcvdRIKEKDRLYSH 874
Cdd:pfam02463  247 R---DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER-----RKVDDEEKLKE 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   875 HSERCHKEGEKIKNITTVKKTDDREKSREKIDRKHDKEKPEKERHLAENKEKHLIEKKNKQADNSDYTKSEKSKNKEKDR 954
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511836369   955 EVDKKEKSRDKEGVNITNTKHIQEEKKSSIADSSKAQHEKTLSL-----KEKTKDEPLKTPDGKEKDKKDKDIDRYKERD 1029
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKqgkltEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          330
                   ....*....|....*...
gi 511836369  1030 KHKDKIQLNSLLKVKSEA 1047
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLE 496
 
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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