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Conserved domains on  [gi|134948605|ref|NP_001077094|]
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ankyrin repeat domain-containing protein 12 isoform 2 [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];
150-268 6.80e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  150 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 229
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  230 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
PTZ00121 super family cl31754
MAEBL; Provisional
 697-1142 8.69e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  697 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 776
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  777 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 856
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  857 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 936
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  937 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1016
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605 1017 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1096
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 134948605 1097 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1142
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 ...
 340-960 2.13e-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: 43.42  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   340 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 419
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   420 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 499
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   500 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 579
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   580 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 646
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   647 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 721
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   722 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 800
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   801 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 880
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   881 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 960
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-268 6.80e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  150 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 229
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  230 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-254 1.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   166 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 245
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 134948605   246 LLLRHGGNP 254
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 155-267 5.25e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 230
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  231 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 267
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PTZ00121 PTZ00121
MAEBL; Provisional
 697-1142 8.69e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  697 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 776
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  777 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 856
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  857 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 936
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  937 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1016
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605 1017 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1096
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 134948605 1097 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1142
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 ...
 693-1026 1.90e-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: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   693 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 772
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   773 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 851
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   852 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 931
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   932 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1009
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 134948605  1010 HKDKIQINSLLKLKSEA 1026
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 162-233 1.11e-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: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  162 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 227
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 134948605  228 DDTPLH 233
Cdd:cd22192   169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 195-222 2.81e-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: 2.81e-05
                            10        20
                    ....*....|....*....|....*...
gi 134948605    195 GWTPLHEACNVGYYDVAKILIAAGADVN 222
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 696-960 1.58e-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: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   696 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 770
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   771 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 844
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   845 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 924
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 134948605   925 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 960
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 340-960 2.13e-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: 43.42  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   340 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 419
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   420 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 499
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   500 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 579
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   580 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 646
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   647 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 721
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   722 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 800
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   801 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 880
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   881 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 960
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-268 6.80e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  150 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 229
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  230 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
151-268 1.81e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  151 QKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 230
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 134948605  231 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-288 8.43e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 8.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 234
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 134948605  235 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDE 288
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-268 7.43e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 7.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  152 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 231
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 134948605  232 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-254 1.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   166 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 245
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 134948605   246 LLLRHGGNP 254
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-263 1.31e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 234
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          90       100
                  ....*....|....*....|....*....
gi 134948605  235 SASSGHRDIVKLLLRHGGNPFQANKHGER 263
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 155-267 5.25e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 230
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  231 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 267
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-224 3.46e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 3.46e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   155 VNKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 224
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 154-268 7.11e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 7.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  154 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 233
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 134948605  234 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-253 1.58e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   97 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPNHPSQTTPAQKKTPSS-----SSRQKDkVNKRNERGETPLHM 168
Cdd:PHA03100   69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  169 AAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 230
Cdd:PHA03100  148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                         170       180
                  ....*....|....*....|...
gi 134948605  231 PLHDSASSGHRDIVKLLLRHGGN 253
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 124-253 1.23e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  124 DNSPDSTPNHPSQTTPAQKKTPSSSSRQKDkVNKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPLHEA 202
Cdd:PHA02876  270 DDCKNTPLHHASQAPSLSRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 134948605  203 CNVGYY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 253
Cdd:PHA02876  349 STLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 93-261 2.53e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 72.24  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   93 GNKKSTPVSILFgyplserKQMALLMQMTARDNSPDSTpnhpSQTTPAQKKTPSSSSRQKDKVNkrnergETPLHMAAIR 172
Cdd:PTZ00322   23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHLEA----LEATENKDATPDHNLTTEEVID------PVVAHMLTVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  173 -------GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVK 245
Cdd:PTZ00322   86 lcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                         170
                  ....*....|....*.
gi 134948605  246 LLLRHGGNPFQANKHG 261
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-268 1.01e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  152 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 231
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 134948605  232 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-268 2.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  123 RDNSPDSTPNHPSQTTPAQKKTPSSSSRQKdKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 202
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  203 cnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:PHA02878  242 --VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-268 2.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 234
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 134948605  235 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:PHA02874  261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 155-251 7.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNE-RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 233
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90
                  ....*....|....*....
gi 134948605  234 DSASS-GHRDIVKLLLRHG 251
Cdd:PHA02878  240 ISVGYcKDYDILKLLLEHG 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 163-250 7.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  163 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 239
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90
                  ....*....|.
gi 134948605  240 HRDIVKLLLRH 250
Cdd:PHA02875  147 DIKGIELLIDH 157
PTZ00121 PTZ00121
MAEBL; Provisional
 697-1142 8.69e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  697 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 776
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  777 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 856
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  857 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 936
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  937 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1016
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605 1017 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1096
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 134948605 1097 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1142
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PHA03095 PHA03095
ankyrin-like protein; Provisional
 155-264 9.69e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 227
Cdd:PHA03095  110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 134948605  228 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 264
Cdd:PHA03095  187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 174-253 1.59e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  174 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 249
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                  ....
gi 134948605  250 HGGN 253
Cdd:PHA03095  106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-215 1.62e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.62e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 134948605   164 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 215
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-248 2.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.12e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 134948605   195 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 248
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 711-1045 1.68e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  711 KSTKEKHVSKERNFKEER--DKIKKESEKSFREEKIKDLKEERENIPTDKdseftslgmsaIEESIGLHLVEKEIDIEKQ 788
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRK-----------FEEARMAHFARRQAAIKAE 1275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  789 EKHIKESKEKPEKRSQIKEKDIEKMERKTFEKekkikhehkseKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNT 868
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEA-----------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  869 AAIKKTDDrEKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESin 948
Cdd:PTZ00121 1345 AEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-- 1421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  949 itNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQinsllKLKSEADK 1028
Cdd:PTZ00121 1422 --EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEE 1494

                         330
                  ....*....|....*..
gi 134948605 1029 PKPKSSPASKDTRPKEK 1045
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 ...
 693-1026 1.90e-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: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   693 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 772
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   773 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 851
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   852 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 931
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   932 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1009
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 134948605  1010 HKDKIQINSLLKLKSEA 1026
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 174-268 2.68e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  174 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 252
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90
                  ....*....|....*.
gi 134948605  253 NPFQANKHGERPVDVA 268
Cdd:PHA02878  226 STDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-223 3.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  154 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 223
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00121 PTZ00121
MAEBL; Provisional
 346-981 1.67e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.07  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  346 EEINKMIDDRHIlRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTSCSVIPE 425
Cdd:PTZ00121 1191 EELRKAEDARKA-EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  426 TS-NSDMQTKKEYVVSGEHKQKGKVKRKLKNQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFRKSFSP 504
Cdd:PTZ00121 1270 AAiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  505 KDDTSlhlfhistgKSPKHSCGLSEKQSTPLKQEHTKTclspGSSEMSLQPDLVR-YDNTESEFLPESSSVKSCKHKEKS 583
Cdd:PTZ00121 1350 AEAEA---------AADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKkADEAKKKAEEDKKKADELKKAAAA 1416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  584 KHQKDfhlEFGEKSNAKIKDEDHSPTFENSdctlKKMDKEGKTLKKHKLKHKEREKEKHKKEIEGEKEKYKTKDSAKELQ 663
Cdd:PTZ00121 1417 KKKAD---EAKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  664 RSVEFDREFWKENFFKSDE---TEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKI--KKESEKS 738
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEA 1569

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  739 FREekikdlkEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEkqekhikESKEKPEKRSQIKEKDIEKMERKTF 818
Cdd:PTZ00121 1570 KKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-------EAKKAEEAKIKAEELKKAEEEKKKV 1635

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  819 EKEKKIKHEHKSEKDKLDLSECVDKIKEKDklyshhtEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD--------K 890
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAE-------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkaeelK 1708

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  891 EKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQ 970
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788

                         650
                  ....*....|.
gi 134948605  971 HEKPLSLKEKT 981
Cdd:PTZ00121 1789 DEKRRMEVDKK 1799
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-202 2.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 134948605   155 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 202
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 95-252 2.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   95 KKSTPVSILF--GYplsERKQMALLMQMTARDNSPDS---TPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMA 169
Cdd:PHA02876  306 KGETPLYLMAknGY---DTENIRTLIMLGADVNAADRlyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  170 AIRGDV----------------------------------KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKIL 214
Cdd:PHA02876  383 AVRNNVviintlldygadiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEML 462

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 134948605  215 IAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 252
Cdd:PHA02876  463 LDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-232 2.94e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 2.94e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134948605  154 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 232
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 164-253 3.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  164 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 242
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                          90
                  ....*....|.
gi 134948605  243 IVKLLLRHGGN 253
Cdd:PHA02875  217 IVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 166-229 5.03e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 5.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134948605  166 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 229
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 161-262 1.13e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  161 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 223
Cdd:PLN03192  557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 134948605  224 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 262
Cdd:PLN03192  637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 685-984 1.50e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.51  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  685 DLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSK--ERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTdkdsef 762
Cdd:PTZ00108 1089 DYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKT------ 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  763 tslgmsaieesiglhlveKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVD 842
Cdd:PTZ00108 1163 ------------------KGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSD 1224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  843 KIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKtdDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSK 922
Cdd:PTZ00108 1225 QEDDEEQKTKPKKSSVKRLKSKKNNSSKSSE--DNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134948605  923 SEKGKNKEKDRE---LDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDE 984
Cdd:PTZ00108 1303 SSPTKKKVKKRLegsLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 155-261 2.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  155 VNKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 223
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 134948605  224 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 261
Cdd:PHA02859  119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-268 2.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 134948605   214 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-249 2.98e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  120 MTARDNSPDSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWT 197
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 134948605  198 PLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLR 249
Cdd:PHA03095  260 PLHYA---AVFNnprACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 161-192 5.33e-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: 5.33e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 134948605   161 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 192
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00121 PTZ00121
MAEBL; Provisional
 643-1041 6.96e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  643 KKEIEGEKEKYKTKDSAKELQRSVEFDR--EFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDD---KSTKEKH 717
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeakKKAEEAK 1483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  718 VSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKhIKESKE 797
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAEE 1562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  798 KPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKE--KDKLYSHHTEKCHKEGEKSKNTAAIKKTD 875
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  876 DREKSREKMDRKHDKEKPEKERHLAESKEkhlmEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHI 955
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  956 QEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSP 1035
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798


                  ....*.
gi 134948605 1036 ASKDTR 1041
Cdd:PTZ00121 1799 KIKDIF 1804
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 160-268 8.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  160 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 239
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100
                  ....*....|....*....|....*....
gi 134948605  240 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 268
Cdd:PHA02875  180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 162-233 1.11e-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: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  162 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 227
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 134948605  228 DDTPLH 233
Cdd:cd22192   169 GNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-268 1.17e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 134948605  211 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 268
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 195-222 1.38e-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: 1.38e-05
                           10        20
                   ....*....|....*....|....*....
gi 134948605   195 GWTPLHEAC-NVGYYDVAKILIAAGADVN 222
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 164-253 1.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  164 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSAS- 237
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISk 116

                          90
                  ....*....|....*..
gi 134948605  238 -SGHRDIVKLLLRHGGN 253
Cdd:PHA03100  117 kSNSYSIVEYLLDNGAN 133
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
675-984 1.90e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  675 ENFFKSDETEDL----FLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFRE-----EKIK 745
Cdd:PRK03918  138 DAILESDESREKvvrqILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineisSELP 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  746 DLKEERENIPTDKDSeftslgMSAIEESIGlhlvEKEIDIEKQEKHIKESKEK---PEKRSQIKEKDIEKMERKTfekek 822
Cdd:PRK03918  218 ELREELEKLEKEVKE------LEELKEEIE----ELEKELESLEGSKRKLEEKireLEERIEELKKEIEELEEKV----- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  823 kikhehksekdkldlsECVDKIKEKDKLYS--------HHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD---KE 891
Cdd:PRK03918  283 ----------------KELKELKEKAEEYIklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKK 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  892 KPEKERHLAESKEKHLM--EKKNKQSDNSEYSKSEKGKNKEK-DRELDKKEKSRDK--ESIN-----ITNSKHIQEEKKS 961
Cdd:PRK03918  347 LKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEieEEISkitarIGELKKEIKELKK 426

                         330       340
                  ....*....|....*....|...
gi 134948605  962 SIVDGNKAQHEKPLSLKEKTKDE 984
Cdd:PRK03918  427 AIEELKKAKGKCPVCGRELTEEH 449
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 178-265 2.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  178 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 257
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                  ....*...
gi 134948605  258 NKHGERPV 265
Cdd:PHA02874  187 DNNGESPL 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 195-222 2.81e-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: 2.81e-05
                            10        20
                    ....*....|....*....|....*...
gi 134948605    195 GWTPLHEACNVGYYDVAKILIAAGADVN 222
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 ...
 651-980 3.03e-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: 49.20  E-value: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   651 EKYKTKDSAKELQRsvefdrefwkenffKSDETEDLFLnmEHESLTLEKKSKLEKNIKDDKSTKEKhvSKERNFKEERDK 730
Cdd:pfam02463  198 QELKLKEQAKKALE--------------YYQLKEKLEL--EEEYLLYLDYLKLNEERIDLLQELLR--DEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   731 IKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLgmSAIEESIGLHLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDI 810
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   811 EK----MERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDR 886
Cdd:pfam02463  338 EElekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   887 KHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDG 966
Cdd:pfam02463  418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497

                          330
                   ....*....|....
gi 134948605   967 NKAQHEKPLSLKEK 980
Cdd:pfam02463  498 RSQKESKARSGLKV 511
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 142-253 3.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  142 KKTPSSSSRQKDKVNKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 216
Cdd:PHA02876  126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 134948605  217 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 253
Cdd:PHA02876  200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
186-233 4.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 4.03e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 134948605   186 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 233
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-254 4.25e-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: 4.25e-05
                            10        20
                    ....*....|....*....|....*...
gi 134948605    227 DDDTPLHDSASSGHRDIVKLLLRHGGNP 254
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 161-190 4.42e-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: 4.42e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 134948605    161 RGETPLHMAAIRGDVKQVKELISLGANVNV 190
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-259 1.97e-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: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 134948605   227 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 259
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-247 2.63e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134948605  169 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 247
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-192 2.85e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 2.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 134948605   153 DKVNKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 192
Cdd:pfam12796   51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 161-190 3.99e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 3.99e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 134948605   161 RGETPLHMAAIRGDVKQVKELISLGANVNV 190
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 175-261 4.15e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  175 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 243
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                          90
                  ....*....|....*...
gi 134948605  244 VKLLLRHGGNPFQANKHG 261
Cdd:PHA02798  128 LLFMIENGADTTLLDKDG 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 195-223 4.27e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.27e-04
                           10        20
                   ....*....|....*....|....*....
gi 134948605   195 GWTPLHEACNVGYYDVAKILIAAGADVNT 223
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 696-960 1.58e-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: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   696 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 770
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   771 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 844
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   845 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 924
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 134948605   925 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 960
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 680-812 1.90e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  680 SDETEDLFLNMEHESLTLEKKSK-LEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFReEKIKDLKEERENIPTDk 758
Cdd:PRK00409  515 KEKLNELIASLEELERELEQKAEeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAIKEAKKEADEIIKE- 592

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 134948605  759 dseftslgMSAIEESIGLHLVEKEIdIEKQeKHIKESKEKPEKRSQIKEKDIEK 812
Cdd:PRK00409  593 --------LRQLQKGGYASVKAHEL-IEAR-KRLNKANEKKEKKKKKQKEKQEE 636
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 340-960 2.13e-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: 43.42  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   340 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 419
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   420 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 499
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   500 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 579
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   580 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 646
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   647 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 721
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   722 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 800
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   801 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 880
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605   881 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 960
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-182 2.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 2.38e-03
                           10        20
                   ....*....|....*....|....*...
gi 134948605   155 VNKRNERGETPLHMAAIRGDVKQVKELI 182
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 162-254 3.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  162 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 240
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                          90
                  ....*....|....
gi 134948605  241 RDIVKLLLRHGGNP 254
Cdd:PHA02875  115 LDIMKLLIARGADP 128
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 690-1040 9.91e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  690 MEHESLTLEKKSKLEKNIKDDKS----TKEKHVSKE---RNFKEERDKIKKESEKSFREEkikdlkEERENIPTDKDSEF 762
Cdd:PTZ00108 1004 LERELARLSNKVRFIKHVINGELvitnAKKKDLVKElkkLGYVRFKDIIKKKSEKITAEE------EEGAEEDDEADDED 1077

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  763 TSLGMSAIEESIglHLVEKEI---DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehksEKDKLDLS- 838
Cdd:PTZ00108 1078 DEEELGAAVSYD--YLLSMPIwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLE--------------DLDKFEEAl 1141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  839 ECVDKIKEKDKLYSHHTEKchKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKK--NKQSD 916
Cdd:PTZ00108 1142 EEQEEVEEKEIAKEQRLKS--KTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdNKKSN 1219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134948605  917 NSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKE--- 993
Cdd:PTZ00108 1220 SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESngg 1299

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134948605  994 -----------------KDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSPASKDT 1040
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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