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Conserved domains on  [gi|1034603732|ref|XP_016881151|]
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ankyrin repeat domain-containing protein 12 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
171-289 6.87e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  171 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 250
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  251 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
PTZ00121 super family cl31754
MAEBL; Provisional
 718-1163 6.72e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 6.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  718 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 797
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  798 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 877
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  878 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 957
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  958 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1037
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732 1038 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1117
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603732 1118 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1163
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 361-981 1.45e-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.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  361 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 440
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  441 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 520
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  521 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 600
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  601 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 667
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  668 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 742
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  743 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 821
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  822 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 901
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  902 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
171-289 6.87e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  171 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 250
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  251 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-275 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 1034603732  187 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 266
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1034603732  267 LLLRHGGNP 275
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 176-288 5.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 251
Cdd:PHA03095    40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  252 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 288
Cdd:PHA03095   120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PTZ00121 PTZ00121
MAEBL; Provisional
 718-1163 6.72e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 6.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  718 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 797
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  798 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 877
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  878 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 957
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  958 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1037
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732 1038 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1117
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603732 1118 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1163
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 714-1047 1.61e-08

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: 59.99  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  714 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 793
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  794 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 872
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  873 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 952
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  953 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1030
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 1034603732 1031 HKDKIQINSLLKLKSEA 1047
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-254 1.12e-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: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  183 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 248
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*.
gi 1034603732  249 DDTPLH 254
Cdd:cd22192    169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-243 2.84e-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: 2.84e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603732   216 GWTPLHEACNVGYYDVAKILIAAGADVN 243
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 361-981 1.45e-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: 43.81  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  361 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 440
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  441 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 520
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  521 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 600
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  601 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 667
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  668 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 742
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  743 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 821
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  822 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 901
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  902 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 717-981 1.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  717 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 791
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  792 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 865
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  866 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 945
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034603732  946 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
171-289 6.87e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  171 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 250
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  251 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-289 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 1034603732  172 QKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 251
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034603732  252 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666    156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
176-309 8.44e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 8.44e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 255
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034603732  256 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDE 309
Cdd:COG0666    226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-289 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 1034603732  173 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 252
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603732  253 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666    124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-275 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 1034603732  187 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 266
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1034603732  267 LLLRHGGNP 275
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
176-284 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 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 255
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                           90       100
                   ....*....|....*....|....*....
gi 1034603732  256 SASSGHRDIVKLLLRHGGNPFQANKHGER 284
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 176-288 5.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 251
Cdd:PHA03095    40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  252 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 288
Cdd:PHA03095   120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-245 3.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 3.49e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 245
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-289 7.19e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 7.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  175 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 254
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034603732  255 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 149-274 8.10e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 8.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  149 NSTPNHPSQTTPAQKKTPSSSSRQKDkVNKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPLHEACNVG 227
Cdd:PHA02876   274 NTPLHHASQAPSLSRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLD 352

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034603732  228 YY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 274
Cdd:PHA02876   353 RNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-274 1.74e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  175 KVNKRNERGETPLHMAAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 236
Cdd:PHA03100   133 NVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034603732  237 AAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 274
Cdd:PHA03100   213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-282 2.03e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 72.62  E-value: 2.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  116 GNKKSTPVSILFgyplserKQMALLMQMTARDNNSTpnHPSQTTPAQKKTPSSSSRQKDKVNkrnergETPLHMAAIR-- 193
Cdd:PTZ00322    23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHL--EALEATENKDATPDHNLTTEEVID------PVVAHMLTVElc 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  194 -----GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 268
Cdd:PTZ00322    88 qlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                          170
                   ....*....|....
gi 1034603732  269 LRHGGNPFQANKHG 282
Cdd:PTZ00322   168 SRHSQCHFELGANA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-289 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 1034603732  173 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 252
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603732  253 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 141-289 1.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  141 MQMTARDNNSTPNHPSQTTPAQKKTPSSSSRQKdKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPL 220
Cdd:PHA02878   160 INMKDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034603732  221 HEAcnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:PHA02878   239 HIS--VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-289 2.54e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 255
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034603732  256 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:PHA02874   261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PTZ00121 PTZ00121
MAEBL; Provisional
 718-1163 6.72e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 6.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  718 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 797
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  798 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 877
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  878 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 957
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  958 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1037
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732 1038 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1117
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603732 1118 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1163
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 184-271 7.42e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 7.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  184 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 260
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90
                   ....*....|.
gi 1034603732  261 HRDIVKLLLRH 271
Cdd:PHA02875   147 DIKGIELLIDH 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 176-285 9.80e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 9.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 248
Cdd:PHA03095   110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603732  249 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 285
Cdd:PHA03095   187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 195-274 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 1034603732  195 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 270
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                   ....
gi 1034603732  271 HGGN 274
Cdd:PHA03095   106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
185-236 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 1034603732  185 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 236
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
216-269 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 1034603732  216 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 269
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 732-1066 1.31e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  732 KSTKEKHVSKERNFKEER--DKIKKESEKSFREEKIKDLKEERENIPTDKdseftslgmsaIEESIGLHLVEKEIDIEKQ 809
Cdd:PTZ00121  1207 KAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRK-----------FEEARMAHFARRQAAIKAE 1275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  810 EKHIKESKEKPEKRSQIKEKDIEKMERKTFEKekkikhehkseKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNT 889
Cdd:PTZ00121  1276 EARKADELKKAEEKKKADEAKKAEEKKKADEA-----------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  890 AAIKKTDDrEKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESin 969
Cdd:PTZ00121  1345 AEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-- 1421

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  970 itNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQinsllKLKSEADK 1049
Cdd:PTZ00121  1422 --EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEE 1494

                          330
                   ....*....|....*..
gi 1034603732 1050 PKPKSSPASKDTRPKEK 1066
Cdd:PTZ00121  1495 AKKKADEAKKAAEAKKK 1511
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 714-1047 1.61e-08

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: 59.99  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  714 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 793
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  794 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 872
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  873 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 952
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  953 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1030
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 1034603732 1031 HKDKIQINSLLKLKSEA 1047
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 195-289 2.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  195 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 273
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90
                   ....*....|....*.
gi 1034603732  274 NPFQANKHGERPVDVA 289
Cdd:PHA02878   226 STDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-244 3.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.23e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  175 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 244
Cdd:PHA03100   184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00121 PTZ00121
MAEBL; Provisional
 367-1002 1.17e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  367 EEINKMIDDRHIlRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTSCSVIPE 446
Cdd:PTZ00121  1191 EELRKAEDARKA-EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  447 TS-NSDMQTKKEYVVSGEHKQKGKVKRKLKNQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFRKSFSP 525
Cdd:PTZ00121  1270 AAiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  526 KDDTSlhlfhistgKSPKHSCGLSEKQSTPLKQEHTKTclspGSSEMSLQPDLVR-YDNTESEFLPESSSVKSCKHKEKS 604
Cdd:PTZ00121  1350 AEAEA---------AADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKkADEAKKKAEEDKKKADELKKAAAA 1416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  605 KHQKDfhlEFGEKSNAKIKDEDHSPTFENSdctlKKMDKEGKTLKKHKLKHKEREKEKHKKEIEGEKEKYKTKDSAKELQ 684
Cdd:PTZ00121  1417 KKKAD---EAKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  685 RSVEFDREFWKENFFKSDE---TEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKI--KKESEKS 759
Cdd:PTZ00121  1490 KKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEA 1569

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  760 FREekikdlkEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEkqekhikESKEKPEKRSQIKEKDIEKMERKTF 839
Cdd:PTZ00121  1570 KKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-------EAKKAEEAKIKAEELKKAEEEKKKV 1635

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  840 EKEKKIKHEHKSEKDKLDLSECVDKIKEKDklyshhtEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD--------K 911
Cdd:PTZ00121  1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAE-------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkaeelK 1708

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  912 EKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQ 991
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788

                          650
                   ....*....|.
gi 1034603732  992 HEKPLSLKEKT 1002
Cdd:PTZ00121  1789 DEKRRMEVDKK 1799
Ank_5 pfam13857
Ankyrin repeats (many copies);
176-223 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 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 223
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-253 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 1034603732  175 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 253
Cdd:COG0666    211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 185-274 3.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  185 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 263
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                           90
                   ....*....|.
gi 1034603732  264 IVKLLLRHGGN 274
Cdd:PHA02875   217 IVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 187-250 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 1034603732  187 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 250
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 151-273 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  151 TPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDV---------------------------------- 196
Cdd:PHA02876   343 TPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVviintlldygadiealsqkigtalhfalcgtnpy 422

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603732  197 KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKILIAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 273
Cdd:PHA02876   423 MSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 185-274 1.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  185 TPLH-----MAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACN--VGYYDVAKILIAAGADVNTQGLDDDTPLHDSA 257
Cdd:PHA03100    70 TPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                           90
                   ....*....|....*....
gi 1034603732  258 SSGHRD--IVKLLLRHGGN 274
Cdd:PHA03100   150 ESNKIDlkILKLLIDKGVD 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 182-283 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 1034603732  182 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 244
Cdd:PLN03192   557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034603732  245 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 283
Cdd:PLN03192   637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 706-1005 1.52e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.51  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  706 DLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSK--ERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTdkdsef 783
Cdd:PTZ00108  1089 DYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKT------ 1162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  784 tslgmsaieesiglhlveKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVD 863
Cdd:PTZ00108  1163 ------------------KGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSD 1224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  864 KIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKtdDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSK 943
Cdd:PTZ00108  1225 QEDDEEQKTKPKKSSVKRLKSKKNNSSKSSE--DNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034603732  944 SEKGKNKEKDRE---LDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDE 1005
Cdd:PTZ00108  1303 SSPTKKKVKKRLegsLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
Ank_5 pfam13857
Ankyrin repeats (many copies);
235-289 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 1034603732  235 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 176-282 2.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  176 VNKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 244
Cdd:PHA02859    44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034603732  245 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 282
Cdd:PHA02859   119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
PTZ00121 PTZ00121
MAEBL; Provisional
 664-1062 5.29e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 5.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  664 KKEIEGEKEKYKTKDSAKELQRSVEFDR--EFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDD---KSTKEKH 738
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeakKKAEEAK 1483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  739 VSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKhIKESKE 818
Cdd:PTZ00121  1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAEE 1562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  819 KPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKE--KDKLYSHHTEKCHKEGEKSKNTAAIKKTD 896
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  897 DREKSREKMDRKHDKEKPEKERHLAESKEkhlmEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHI 976
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  977 QEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSP 1056
Cdd:PTZ00121  1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798


                   ....*.
gi 1034603732 1057 ASKDTR 1062
Cdd:PTZ00121  1799 KIKDIF 1804
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-213 5.38e-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: 5.38e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034603732  182 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 213
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 181-289 8.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 8.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  181 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 260
Cdd:PHA02875   100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                           90       100
                   ....*....|....*....|....*....
gi 1034603732  261 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 289
Cdd:PHA02875   180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
PHA03095 PHA03095
ankyrin-like protein; Provisional
 143-270 1.05e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  143 MTARDN--NSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWT 218
Cdd:PHA03095   180 VYAVDDrfRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034603732  219 PLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLR 270
Cdd:PHA03095   260 PLHYA---AVFNnprACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-254 1.12e-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: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  183 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 248
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*.
gi 1034603732  249 DDTPLH 254
Cdd:cd22192    169 GNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 232-289 1.18e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603732  232 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 289
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-243 1.39e-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: 1.39e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034603732  216 GWTPLHEAC-NVGYYDVAKILIAAGADVN 243
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
696-1005 1.53e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  696 ENFFKSDETED----LFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFRE-----EKIK 766
Cdd:PRK03918   138 DAILESDESREkvvrQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineisSELP 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  767 DLKEERENIPTDKDSeftslgMSAIEESIGlhlvEKEIDIEKQEKHIKESKEK---PEKRSQIKEKDIEKMERKTfekek 843
Cdd:PRK03918   218 ELREELEKLEKEVKE------LEELKEEIE----ELEKELESLEGSKRKLEEKireLEERIEELKKEIEELEEKV----- 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  844 kikhehksekdkldlsECVDKIKEKDKLYS--------HHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD---KE 912
Cdd:PRK03918   283 ----------------KELKELKEKAEEYIklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKK 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  913 KPEKERHLAESKEKHLM--EKKNKQSDNSEYSKSEKGKNKEK-DRELDKKEKSRDK--ESIN-----ITNSKHIQEEKKS 982
Cdd:PRK03918   347 LKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEieEEISkitarIGELKKEIKELKK 426

                          330       340
                   ....*....|....*....|...
gi 1034603732  983 SIVDGNKAQHEKPLSLKEKTKDE 1005
Cdd:PRK03918   427 AIEELKKAKGKCPVCGRELTEEH 449
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 185-274 1.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  185 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSAS- 258
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISk 116

                           90
                   ....*....|....*..
gi 1034603732  259 -SGHRDIVKLLLRHGGN 274
Cdd:PHA03100   117 kSNSYSIVEYLLDNGAN 133
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 199-286 2.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  199 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 278
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                   ....*...
gi 1034603732  279 NKHGERPV 286
Cdd:PHA02874   187 DNNGESPL 194
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 672-981 2.42e-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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.58  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  672 EKYKTKDSAKELQRsvefdrefwkenffKSDETEDLFLnmEHESLTLEKKSKLEKNIKDDKSTKEKhvSKERNFKEERDK 751
Cdd:pfam02463  198 QELKLKEQAKKALE--------------YYQLKEKLEL--EEEYLLYLDYLKLNEERIDLLQELLR--DEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  752 IKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLgmSAIEESIGLHLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDI 831
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  832 EK----MERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDR 907
Cdd:pfam02463  338 EElekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603732  908 KHDKEKPEKERHLAESKEKHLMEKK----NKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:pfam02463  418 EDLLKEEKKEELEILEEEEESIELKqgklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-243 2.84e-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: 2.84e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603732   216 GWTPLHEACNVGYYDVAKILIAAGADVN 243
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 163-274 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  163 KKTPSSSSRQKDKVNKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 237
Cdd:PHA02876   126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603732  238 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 274
Cdd:PHA02876   200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
207-254 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 1034603732  207 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 254
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 248-275 4.29e-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: 4.29e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603732   248 DDDTPLHDSASSGHRDIVKLLLRHGGNP 275
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-211 4.46e-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: 4.46e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1034603732   182 RGETPLHMAAIRGDVKQVKELISLGANVNV 211
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 248-280 1.99e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.99e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034603732  248 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 280
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 190-268 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 1034603732  190 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 268
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-213 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 1034603732  174 DKVNKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 213
Cdd:pfam12796   51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-211 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 1034603732  182 RGETPLHMAAIRGDVKQVKELISLGANVNV 211
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 196-282 4.30e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  196 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 264
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                           90
                   ....*....|....*...
gi 1034603732  265 VKLLLRHGGNPFQANKHG 282
Cdd:PHA02798   128 LLFMIENGADTTLLDKDG 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-244 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 1034603732  216 GWTPLHEACNVGYYDVAKILIAAGADVNT 244
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 361-981 1.45e-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: 43.81  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  361 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 440
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  441 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 520
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  521 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 600
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  601 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 667
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  668 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 742
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  743 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 821
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  822 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 901
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  902 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 717-981 1.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  717 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 791
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  792 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 865
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  866 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 945
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034603732  946 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 981
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 701-833 1.82e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  701 SDETEDLFLNMEHESLTLEKKSK-LEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFReEKIKDLKEERENIPTDk 779
Cdd:PRK00409   515 KEKLNELIASLEELERELEQKAEeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAIKEAKKEADEIIKE- 592

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034603732  780 dseftslgMSAIEESIGLHLVEKEIdIEKQeKHIKESKEKPEKRSQIKEKDIEK 833
Cdd:PRK00409   593 --------LRQLQKGGYASVKAHEL-IEAR-KRLNKANEKKEKKKKKQKEKQEE 636
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-203 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 1034603732  176 VNKRNERGETPLHMAAIRGDVKQVKELI 203
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 183-275 3.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  183 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 261
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                           90
                   ....*....|....
gi 1034603732  262 RDIVKLLLRHGGNP 275
Cdd:PHA02875   115 LDIMKLLIARGADP 128
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 711-1061 9.21e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  711 MEHESLTLEKKSKLEKNIKDDKS----TKEKHVSKE---RNFKEERDKIKKESEKSFREEkikdlkEERENIPTDKDSEF 783
Cdd:PTZ00108  1004 LERELARLSNKVRFIKHVINGELvitnAKKKDLVKElkkLGYVRFKDIIKKKSEKITAEE------EEGAEEDDEADDED 1077

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  784 TSLGMSAIEESIglHLVEKEI---DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehksEKDKLDLS- 859
Cdd:PTZ00108  1078 DEEELGAAVSYD--YLLSMPIwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLE--------------DLDKFEEAl 1141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  860 ECVDKIKEKDKLYSHHTEKchKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKK--NKQSD 937
Cdd:PTZ00108  1142 EEQEEVEEKEIAKEQRLKS--KTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdNKKSN 1219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603732  938 NSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKE--- 1014
Cdd:PTZ00108  1220 SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESngg 1299

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034603732 1015 -----------------KDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSPASKDT 1061
Cdd:PTZ00108  1300 skpssptkkkvkkrlegSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDS 1363
 
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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