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Conserved domains on  [gi|398366259|ref|NP_011754|]
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Kel2p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
77-391 9.95e-25

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 104.85  E-value: 9.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  77 KLKNSPFPRyRHSSSFIVtnDNRIFVTGGLHDQSVYGDVWqiaanadgtsftskRIDIDQNT-------PPPRVGHAST- 148
Cdd:COG3055    5 SLPDLPTPR-SEAAAALL--DGKVYVAGGLSGGSASNSFE--------------VYDPATNTwselaplPGPPRHHAAAv 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 149 -ICGNAYvVFGGDTHKLNKNGLLdDDLYLFNINSYKWTipqPIGRRPLGRYGHkisiiASNPMQTKLYLFGGQVDETYFN 227
Cdd:COG3055   68 aQDGKLY-VFGGFTGANPSSTPL-NDVYVYDPATNTWT---KLAPMPTPRGGA-----TALLLDGKIYVVGGWDDGGNVA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 228 DLVVFDLSSfrrpNShWeflEPVGDLPPPLTNHT-MVAYDNKLWVFGGetpktisndtYRYDPAQSEWSkvkTTGEKPPP 306
Cdd:COG3055  138 WVEVYDPAT----GT-W---TQLAPLPTPRDHLAaAVLPDGKILVIGG----------RNGSGFSNTWT---TLAPLPTA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 307 IQEHASVVYKHLMCVLGGKdthNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGDKTDYASPN 386
Cdd:COG3055  197 RAGHAAAVLGGKILVFGGE---SGFSDEVEAYDPATNTWTALGEL----PTPRHGHAAVLTDGKVYVIGGETKPGVRTPL 269

                 ....*
gi 398366259 387 IHDLQ 391
Cdd:COG3055  270 VTSAE 274
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
603-872 1.93e-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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   603 ARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQI-TIQNNGLKTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNM 681
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   682 QKITPELHTYLNESSCYLGKLLKSYPTSARPPSSEKDNQIYE-KDSLNKIEKVINEMHetvRAKEKLHLETQKLNDERDS 760
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   761 LRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFD 840
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQIEK 914
                          250       260       270
                   ....*....|....*....|....*....|..
gi 398366259   841 AFHRMKinNLKAELYMSKENRDSLKDELLALK 872
Cdd:TIGR02169  915 KRKRLS--ELKAKLEALEEELSEIEDPKGEDE 944
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
77-391 9.95e-25

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 104.85  E-value: 9.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  77 KLKNSPFPRyRHSSSFIVtnDNRIFVTGGLHDQSVYGDVWqiaanadgtsftskRIDIDQNT-------PPPRVGHAST- 148
Cdd:COG3055    5 SLPDLPTPR-SEAAAALL--DGKVYVAGGLSGGSASNSFE--------------VYDPATNTwselaplPGPPRHHAAAv 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 149 -ICGNAYvVFGGDTHKLNKNGLLdDDLYLFNINSYKWTipqPIGRRPLGRYGHkisiiASNPMQTKLYLFGGQVDETYFN 227
Cdd:COG3055   68 aQDGKLY-VFGGFTGANPSSTPL-NDVYVYDPATNTWT---KLAPMPTPRGGA-----TALLLDGKIYVVGGWDDGGNVA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 228 DLVVFDLSSfrrpNShWeflEPVGDLPPPLTNHT-MVAYDNKLWVFGGetpktisndtYRYDPAQSEWSkvkTTGEKPPP 306
Cdd:COG3055  138 WVEVYDPAT----GT-W---TQLAPLPTPRDHLAaAVLPDGKILVIGG----------RNGSGFSNTWT---TLAPLPTA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 307 IQEHASVVYKHLMCVLGGKdthNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGDKTDYASPN 386
Cdd:COG3055  197 RAGHAAAVLGGKILVFGGE---SGFSDEVEAYDPATNTWTALGEL----PTPRHGHAAVLTDGKVYVIGGETKPGVRTPL 269

                 ....*
gi 398366259 387 IHDLQ 391
Cdd:COG3055  270 VTSAE 274
PLN02153 PLN02153
epithiospecifier protein
139-379 1.67e-20

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 93.90  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 139 PPPRVGHASTICGNAYVVFGGDthkLNKNGLLDDDLYLFNINSYKWTIPQPIGRRP-LGRYGHKISIIAsnpmqTKLYLF 217
Cdd:PLN02153  20 PGPRCSHGIAVVGDKLYSFGGE---LKPNEHIDKDLYVFDFNTHTWSIAPANGDVPrISCLGVRMVAVG-----TKLYIF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 218 GGQVDETYFNDLVVFDLSSfrrpnSHWEFLEPVGDL--PPPLTNHTMVAYDNKLWVFGG-------ETPK---TI----- 280
Cdd:PLN02153  92 GGRDEKREFSDFYSYDTVK-----NEWTFLTKLDEEggPEARTFHSMASDENHVYVFGGvskgglmKTPErfrTIeayni 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 281 -------------------------------------------------SNDTYRYDPAQSEWSKVKTTGEKPPPIQEHA 311
Cdd:PLN02153 167 adgkwvqlpdpgenfekrggagfavvqgkiwvvygfatsilpggksdyeSNAVQFFDPASGKWTEVETTGAKPSARSVFA 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366259 312 SVVYKHLMCVLGGK---DTHNAY-----SNDVYFLNLLSLKWYKLPRMKE-GIPQERSGHSLTLMKNEKLLIMGGDK 379
Cdd:PLN02153 247 HAVVGKYIIIFGGEvwpDLKGHLgpgtlSNEGYALDTETLVWEKLGECGEpAMPRGWTAYTTATVYGKNGLLMHGGK 323
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
603-872 1.93e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   603 ARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQI-TIQNNGLKTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNM 681
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   682 QKITPELHTYLNESSCYLGKLLKSYPTSARPPSSEKDNQIYE-KDSLNKIEKVINEMHetvRAKEKLHLETQKLNDERDS 760
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   761 LRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFD 840
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQIEK 914
                          250       260       270
                   ....*....|....*....|....*....|..
gi 398366259   841 AFHRMKinNLKAELYMSKENRDSLKDELLALK 872
Cdd:TIGR02169  915 KRKRLS--ELKAKLEALEEELSEIEDPKGEDE 944
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
561-827 4.93e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 561 QTLRLEAQQKELEtarhisQLEKEvqrlmvIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLmvklsqaSKLCDQI 640
Cdd:COG4942   18 QADAAAEAEAELE------QLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 641 TIQNNGLKTcsehvtIKRDIIDLENKcdvLKRQNEILVNNMQKItpelhtYLNESSCYLGKLLksyptSARPPSSEKDNQ 720
Cdd:COG4942   79 AALEAELAE------LEKEIAELRAE---LEAQKEELAELLRAL------YRLGRQPPLALLL-----SPEDFLDAVRRL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 721 IYEKDSLNKIEKVINEMHETvraKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSEL 800
Cdd:COG4942  139 QYLKYLAPARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
                        250       260
                 ....*....|....*....|....*..
gi 398366259 801 EKYRKNNDDLQKEIDRIKTEQAEQDDK 827
Cdd:COG4942  216 AELQQEAEELEALIARLEAEAAAAAER 242
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
256-299 1.21e-07

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 48.76  E-value: 1.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 398366259  256 PLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKT 299
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
553-882 4.30e-07

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 53.96  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  553 FDDLNLNLQTLRLEAQQKELETARHISQLEKEVQrlmvikeasKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQ 632
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYK---------KEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  633 ASKLCDQITIQNNGLKTCSE---HVTIKRDIIDLEnkcdvLKRQneilvNNMQKITPELHTYLNESSCYLgkllksypts 709
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEkkdHLTKELEDIKMS-----LQRS-----MSTQKALEEDLQIATKTICQL---------- 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  710 arppSSEKDNQIYEkdsLNKIEK----VINEMHETV-RAKEKLHLETQKLNDERDSLR---ANLLDNNNKLDALRKLSDG 781
Cdd:pfam05483 330 ----TEEKEAQMEE---LNKAKAahsfVVTEFEATTcSLEELLRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNN 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  782 SSKSMDLTKKAIHLSQS---ELEKYRKNNDDL----QKEIDRIKTEQAEQDDKQEQRGAITHGnfDAFHRMKINNLKAEL 854
Cdd:pfam05483 403 KEVELEELKKILAEDEKlldEKKQFEKIAEELkgkeQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTEL 480
                         330       340
                  ....*....|....*....|....*...
gi 398366259  855 ymskeNRDSLKDELLALKKKLYTLEQKK 882
Cdd:pfam05483 481 -----EKEKLKNIELTAHCDKLLLENKE 503
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
727-882 1.37e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.93  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   727 LNKIEKVINEMHET-VRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKsmdltkkaihLSQSELEKYRK 805
Cdd:smart00787 142 LEGLKEGLDENLEGlKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELED----------CDPTELDRAKE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   806 NNDDLQKEIDRIKTEQAE-QDDKQEQRGAITHGNfdafhrMKINNLKAELYMS----KENRDSLKDELLALKKKLYTLEQ 880
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEElEEELQELESKIEDLT------NKKSELNTEIAEAekklEQCRGFTFKEIEKLKEQLKLLQS 285

                   ..
gi 398366259   881 KK 882
Cdd:smart00787 286 LT 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
557-880 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 557 NLNLQTLRLEAQQKELETarHISQLEKEVQRLmviKEASKDSNFQTARLKNLEiQKTFLESRINDLKNLLMVKLSQASKL 636
Cdd:PRK03918 242 ELEKELESLEGSKRKLEE--KIRELEERIEEL---KKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKR 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 637 CDQITIQNNGlktcsehvtIKRDIIDLENKcdvLKRQNEIlvnnmQKITPELHTYLNEsscyLGKLLKSYPTsARPPSSE 716
Cdd:PRK03918 316 LSRLEEEING---------IEERIKELEEK---EERLEEL-----KKKLKELEKRLEE----LEERHELYEE-AKAKKEE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 717 KdNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsdgssksmdlTKKAIHLS 796
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----------AKGKCPVC 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 797 QSEL-EKYRKN-NDDLQKEIDRIKTEQAEQDDKQEQrgaithgnfdafhrMKINNLKAELYMSKENR----DSLKDELLA 870
Cdd:PRK03918 442 GRELtEEHRKElLEEYTAELKRIEKELKEIEEKERK--------------LRKELRELEKVLKKESEliklKELAEQLKE 507
                        330
                 ....*....|..
gi 398366259 871 LKKKL--YTLEQ 880
Cdd:PRK03918 508 LEEKLkkYNLEE 519
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
77-391 9.95e-25

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 104.85  E-value: 9.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  77 KLKNSPFPRyRHSSSFIVtnDNRIFVTGGLHDQSVYGDVWqiaanadgtsftskRIDIDQNT-------PPPRVGHAST- 148
Cdd:COG3055    5 SLPDLPTPR-SEAAAALL--DGKVYVAGGLSGGSASNSFE--------------VYDPATNTwselaplPGPPRHHAAAv 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 149 -ICGNAYvVFGGDTHKLNKNGLLdDDLYLFNINSYKWTipqPIGRRPLGRYGHkisiiASNPMQTKLYLFGGQVDETYFN 227
Cdd:COG3055   68 aQDGKLY-VFGGFTGANPSSTPL-NDVYVYDPATNTWT---KLAPMPTPRGGA-----TALLLDGKIYVVGGWDDGGNVA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 228 DLVVFDLSSfrrpNShWeflEPVGDLPPPLTNHT-MVAYDNKLWVFGGetpktisndtYRYDPAQSEWSkvkTTGEKPPP 306
Cdd:COG3055  138 WVEVYDPAT----GT-W---TQLAPLPTPRDHLAaAVLPDGKILVIGG----------RNGSGFSNTWT---TLAPLPTA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 307 IQEHASVVYKHLMCVLGGKdthNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGDKTDYASPN 386
Cdd:COG3055  197 RAGHAAAVLGGKILVFGGE---SGFSDEVEAYDPATNTWTALGEL----PTPRHGHAAVLTDGKVYVIGGETKPGVRTPL 269

                 ....*
gi 398366259 387 IHDLQ 391
Cdd:COG3055  270 VTSAE 274
PLN02153 PLN02153
epithiospecifier protein
139-379 1.67e-20

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 93.90  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 139 PPPRVGHASTICGNAYVVFGGDthkLNKNGLLDDDLYLFNINSYKWTIPQPIGRRP-LGRYGHKISIIAsnpmqTKLYLF 217
Cdd:PLN02153  20 PGPRCSHGIAVVGDKLYSFGGE---LKPNEHIDKDLYVFDFNTHTWSIAPANGDVPrISCLGVRMVAVG-----TKLYIF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 218 GGQVDETYFNDLVVFDLSSfrrpnSHWEFLEPVGDL--PPPLTNHTMVAYDNKLWVFGG-------ETPK---TI----- 280
Cdd:PLN02153  92 GGRDEKREFSDFYSYDTVK-----NEWTFLTKLDEEggPEARTFHSMASDENHVYVFGGvskgglmKTPErfrTIeayni 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 281 -------------------------------------------------SNDTYRYDPAQSEWSKVKTTGEKPPPIQEHA 311
Cdd:PLN02153 167 adgkwvqlpdpgenfekrggagfavvqgkiwvvygfatsilpggksdyeSNAVQFFDPASGKWTEVETTGAKPSARSVFA 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366259 312 SVVYKHLMCVLGGK---DTHNAY-----SNDVYFLNLLSLKWYKLPRMKE-GIPQERSGHSLTLMKNEKLLIMGGDK 379
Cdd:PLN02153 247 HAVVGKYIIIFGGEvwpDLKGHLgpgtlSNEGYALDTETLVWEKLGECGEpAMPRGWTAYTTATVYGKNGLLMHGGK 323
PLN02193 PLN02193
nitrile-specifier protein
130-379 4.26e-19

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 91.17  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 130 KRIDIDQNT--PPPRVGHASTICGNAYVVFGGDthkLNKNGLLDDDLYLFNINSYKWTIPQPIGRRP-LGRYGHKISIIA 206
Cdd:PLN02193 152 KWIKVEQKGegPGLRCSHGIAQVGNKIYSFGGE---FTPNQPIDKHLYVFDLETRTWSISPATGDVPhLSCLGVRMVSIG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 207 SNpmqtkLYLFGGQVDETYFNDLVVFDLSSfrrpnSHWEFLEPVGDLPPPLTNHTMVAYDNKLWVFGG----ETPKTIS- 281
Cdd:PLN02193 229 ST-----LYVFGGRDASRQYNGFYSFDTTT-----NEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGvsatARLKTLDs 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 282 --------------------------------------------NDTYRYDPAQSEWSKVKTTGEKPPPIQEHAS-VVYK 316
Cdd:PLN02193 299 ynivdkkwfhcstpgdsfsirggaglevvqgkvwvvygfngcevDDVHYYDPVQDKWTQVETFGVRPSERSVFASaAVGK 378
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 317 HLMcVLGGKDTHN--------AYSNDVYFLNLLSLKWYKLPRM--KEGIPQER--SGHSLTLMKNEKLLIMGGDK 379
Cdd:PLN02193 379 HIV-IFGGEIAMDplahvgpgQLTDGTFALDTETLQWERLDKFgeEEETPSSRgwTASTTGTIDGKKGLVMHGGK 452
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
248-378 3.02e-16

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 79.81  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 248 EPVGDLPPPLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKvktTGEKP-PPIQEHASVVYKHLMCVLGGKD 326
Cdd:COG3055    4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSE---LAPLPgPPRHHAAAVAQDGKLYVFGGFT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 327 THNA---YSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGD 378
Cdd:COG3055   81 GANPsstPLNDVYVYDPATNTWTKLAPM----PTPRGGATALLLDGKIYVVGGWD 131
PLN02153 PLN02153
epithiospecifier protein
186-384 4.92e-12

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 68.09  E-value: 4.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 186 IPQPIGRRPLGRYGHKISIIASnpmqtKLYLFGGQV--DETYFNDLVVFDLssfrrpNSH-WEFLEPVGDLPPPLT-NHT 261
Cdd:PLN02153  12 VEQKGGKGPGPRCSHGIAVVGD-----KLYSFGGELkpNEHIDKDLYVFDF------NTHtWSIAPANGDVPRISClGVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 262 MVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKTTGEKPPPIQE--HASVVYKHLMCVLGGKDTHNAYSNDVYF-- 337
Cdd:PLN02153  81 MVAVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGGPEARtfHSMASDENHVYVFGGVSKGGLMKTPERFrt 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366259 338 ---LNLLSLKWYKLPRMKEGIpQERSGHSLTLMKNEKLLIMG-------GDKTDYAS 384
Cdd:PLN02153 161 ieaYNIADGKWVQLPDPGENF-EKRGGAGFAVVQGKIWVVYGfatsilpGGKSDYES 216
PLN02193 PLN02193
nitrile-specifier protein
167-377 2.66e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 60.35  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 167 NGLLDDDLYLFNINSYKWTIPQPIGRRPlgryghkisiiasnpmQTKLYLFGGQVDETYFNDLVVFD-----LSSFRRPN 241
Cdd:PLN02193  85 NDMTSEMITFLSFKTYKGKTSHPIEKRP----------------GVKFVLQGGKIVGFHGRSTDVLHslgayISLPSTPK 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 242 SH--WEFLEPVGDLPPPLTNHTMVAYDNKLWVFGGE-TP-KTISNDTYRYDPAQSEWSKVKTTGEKPppiqehasvvykH 317
Cdd:PLN02193 149 LLgkWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEfTPnQPIDKHLYVFDLETRTWSISPATGDVP------------H 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366259 318 LMC-------------VLGGKDTHNAYsNDVYFLNLLSLKWYKLPRMKEGiPQERSGHSLTlMKNEKLLIMGG 377
Cdd:PLN02193 217 LSClgvrmvsigstlyVFGGRDASRQY-NGFYSFDTTTNEWKLLTPVEEG-PTPRSFHSMA-ADEENVYVFGG 286
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
603-872 1.93e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   603 ARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQI-TIQNNGLKTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNM 681
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   682 QKITPELHTYLNESSCYLGKLLKSYPTSARPPSSEKDNQIYE-KDSLNKIEKVINEMHetvRAKEKLHLETQKLNDERDS 760
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   761 LRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFD 840
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQIEK 914
                          250       260       270
                   ....*....|....*....|....*....|..
gi 398366259   841 AFHRMKinNLKAELYMSKENRDSLKDELLALK 872
Cdd:TIGR02169  915 KRKRLS--ELKAKLEALEEELSEIEDPKGEDE 944
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
561-827 4.93e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 561 QTLRLEAQQKELEtarhisQLEKEvqrlmvIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLmvklsqaSKLCDQI 640
Cdd:COG4942   18 QADAAAEAEAELE------QLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 641 TIQNNGLKTcsehvtIKRDIIDLENKcdvLKRQNEILVNNMQKItpelhtYLNESSCYLGKLLksyptSARPPSSEKDNQ 720
Cdd:COG4942   79 AALEAELAE------LEKEIAELRAE---LEAQKEELAELLRAL------YRLGRQPPLALLL-----SPEDFLDAVRRL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 721 IYEKDSLNKIEKVINEMHETvraKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSEL 800
Cdd:COG4942  139 QYLKYLAPARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
                        250       260
                 ....*....|....*....|....*..
gi 398366259 801 EKYRKNNDDLQKEIDRIKTEQAEQDDK 827
Cdd:COG4942  216 AELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
557-824 9.64e-08

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: 56.22  E-value: 9.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   557 NLNLQTLRLEAQQKELETARH-ISQLEKEV-QRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQAS 634
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKeLEELEEELeQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   635 KLCDQITIQNNGLKTCSEH-VTIKRDIIDLENKCDVLKRQNEILvnNMQkitpelHTYLNESSCYLGKLLKSYPTSARPP 713
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDEL--RAE------LTLLNEEAANLRERLESLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   714 SSEKDNQIYEKDSLNK-IEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALR-KLSDGSSKSMDLTKK 791
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEdIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeELRELESKRSELRRE 916
                          250       260       270
                   ....*....|....*....|....*....|...
gi 398366259   792 AIHLsQSELEKYRKNNDDLQKEIDRIKTEQAEQ 824
Cdd:TIGR02168  917 LEEL-REKLAQLELRLEGLEVRIDNLQERLSEE 948
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
256-299 1.21e-07

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 48.76  E-value: 1.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 398366259  256 PLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKT 299
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
564-882 2.14e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.07  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   564 RLEAQQKELETARHISQLEKEVQ------RLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNllmvKLSQASKLC 637
Cdd:TIGR02169  199 QLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK----RLEEIEQLL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   638 DQITIQNNGLkTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELHTYlnesscylgkllksyptsarppSSEK 717
Cdd:TIGR02169  275 EELNKKIKDL-GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL----------------------EAEI 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   718 DNQIYEKDSLNKiekvinEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsdgssKSMDLtkkaihlsQ 797
Cdd:TIGR02169  332 DKLLAEIEELER------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD------ELKDY--------R 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   798 SELEKYRKNNDDLQKEIDRIkteqaeQDDKQEQRGAIthgnfdAFHRMKINNLKAELYMSKENRDSLKDELLALKKKLYT 877
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRL------QEELQRLSEEL------ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459

                   ....*
gi 398366259   878 LEQKK 882
Cdd:TIGR02169  460 LAADL 464
PRK14131 PRK14131
N-acetylneuraminate epimerase;
240-300 2.38e-07

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 53.87  E-value: 2.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366259 240 PNSHWEflePVGDLPPPLTNH-TMVAYDNKLWVFGG------ETPKTISNDTYRYDPAQSEWSKVKTT 300
Cdd:PRK14131  60 PSKGWT---KIAAFPGGPREQaVAAFIDGKLYVFGGigktnsEGSPQVFDDVYKYDPKTNSWQKLDTR 124
Kelch_4 pfam13418
Galactose oxidase, central domain;
259-299 3.08e-07

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 47.61  E-value: 3.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 398366259  259 NHTMVA-YDNKLWVFGGETPK-TISNDTYRYDPAQSEWSKVKT 299
Cdd:pfam13418   4 YHTSTSiPDDTIYLFGGEGEDgTLLSDLWVFDLSTNEWTRLGS 46
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
553-882 4.30e-07

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 53.96  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  553 FDDLNLNLQTLRLEAQQKELETARHISQLEKEVQrlmvikeasKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQ 632
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYK---------KEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  633 ASKLCDQITIQNNGLKTCSE---HVTIKRDIIDLEnkcdvLKRQneilvNNMQKITPELHTYLNESSCYLgkllksypts 709
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEkkdHLTKELEDIKMS-----LQRS-----MSTQKALEEDLQIATKTICQL---------- 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  710 arppSSEKDNQIYEkdsLNKIEK----VINEMHETV-RAKEKLHLETQKLNDERDSLR---ANLLDNNNKLDALRKLSDG 781
Cdd:pfam05483 330 ----TEEKEAQMEE---LNKAKAahsfVVTEFEATTcSLEELLRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNN 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  782 SSKSMDLTKKAIHLSQS---ELEKYRKNNDDL----QKEIDRIKTEQAEQDDKQEQRGAITHGnfDAFHRMKINNLKAEL 854
Cdd:pfam05483 403 KEVELEELKKILAEDEKlldEKKQFEKIAEELkgkeQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTEL 480
                         330       340
                  ....*....|....*....|....*...
gi 398366259  855 ymskeNRDSLKDELLALKKKLYTLEQKK 882
Cdd:pfam05483 481 -----EKEKLKNIELTAHCDKLLLENKE 503
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
721-882 7.62e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 721 IYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSEL 800
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 801 EKYRKNNDDLQKEIDRIkteQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQ 880
Cdd:COG4372  104 ESLQEEAEELQEELEEL---QKERQDLEQQRKQLEA---------QIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                 ..
gi 398366259 881 KK 882
Cdd:COG4372  172 EL 173
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
555-882 1.90e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.65  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  555 DLNLNLQTLRLEAQQKELETARHISQLEKEVQRLMVIKEASKDSnfQTARLKNLEIQKTFLESRinDLKNLlmvklsQAS 634
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTELEKE--KLKNI------ELT 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  635 KLCDQITIQNNGLKTCSEHVTI-----KRDIIDLENKCDVLKRQNEILV-------NNMQKITPELHTYLNESSCYLGKL 702
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLelkkhQEDIINCKKQEERMLKQIENLEekemnlrDELESVREEFIQKGDEVKCKLDKS 571
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  703 LKSYPT-SARPPSSEKDNQIYEKDSLN---KIE---KVINEMHETVRA-KEKLHLETQKLNDERDSLRANLLDNNNKLDA 774
Cdd:pfam05483 572 EENARSiEYEVLKKEKQMKILENKCNNlkkQIEnknKNIEELHQENKAlKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  775 LRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDD---LQKEID-RIKTEQAEQDDKQEQrgaithgnfdafHRMKINNL 850
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDkRCQHKIAEMVALMEK------------HKHQYDKI 719
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 398366259  851 KAE------LYMSKENRDS------------LKDELLALKKKLYTLEQKK 882
Cdd:pfam05483 720 IEErdselgLYKNKEQEQSsakaaleielsnIKAELLSLKKQLEIEKEEK 769
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
560-825 1.90e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 51.75  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  560 LQTLRLEAQQKELETARHISQLEKEVQrlMVIKEASKDSNFQTARLKNLEIQKT---FLESRINDLKNLLMVKLSQASKL 636
Cdd:pfam10174 231 LQTVIEMKDTKISSLERNIRDLEDEVQ--MLKTNGLLHTEDREEEIKQMEVYKShskFMKNKIDQLKQELSKKESELLAL 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  637 CDQITIQNNGLKTCSEHVTI-KRDIIDLENKCDVLKRQNEILVNNMQkitpELHTYLNESSCYLGKLLKSYPTSARPPSS 715
Cdd:pfam10174 309 QTKLETLTNQNSDCKQHIEVlKESLTAKEQRAAILQTEVDALRLRLE----EKESFLNKKTKQLQDLTEEKSTLAGEIRD 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  716 EKDNQIYEKDSLNKIEKVINEMHETVRAKEKlhletqKLNDERDSLRANLLDNNNKLDALRKLSDGSS---KSMDLTKKA 792
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQLRDKDK------QLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 398366259  793 IHLS----QSELEKYRKNNDDLQKEIDRIKTEQAEQD 825
Cdd:pfam10174 459 REREdrerLEELESLKKENKDLKEKVSALQPELTEKE 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
555-880 2.88e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   555 DLNLNLQTLRLEAQQKELETARhiSQLEKEVQRLmviKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQAS 634
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQ--EELKEAEEEL---EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   635 KLCDQITIQNNGLKtcsehvtikrdiiDLENKcdvLKRQNEILVNNMQKITpELHTYLNESSCYLGKLLKsyptsarpps 714
Cdd:TIGR02168  299 RLEQQKQILRERLA-------------NLERQ---LEELEAQLEELESKLD-ELAEELAELEEKLEELKE---------- 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   715 sEKDNQiyeKDSLNKIEKVINEMHETVRAKEKLHletQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:TIGR02168  352 -ELESL---EAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   795 LSQSELEKYRKnnDDLQKEIDRIKTEQAEQDDKQEqrgaithgnfdaFHRMKINNLKAELYMSKENRDSLKDELLALKKK 874
Cdd:TIGR02168  425 ELLKKLEEAEL--KELQAELEELEEELEELQEELE------------RLEEALEELREELEEAEQALDAAERELAQLQAR 490

                   ....*.
gi 398366259   875 LYTLEQ 880
Cdd:TIGR02168  491 LDSLER 496
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
605-880 5.59e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.50  E-value: 5.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   605 LKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQNNGL--KTCSEHvtiKRDIIDLENKCDVLKRQNEILVNNMQ 682
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieQLISEH---EVEITGLTEKASSARSQANSIQSQLE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   683 KITPELHtylNESSCYLGKL--LKSYPTSARPPSSEKdNQIYEkDSLNKIEKVI----NEMHETVRAKEKLHLETQKLND 756
Cdd:pfam15921  303 IIQEQAR---NQNSMYMRQLsdLESTVSQLRSELREA-KRMYE-DKIEELEKQLvlanSELTEARTERDQFSQESGNLDD 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   757 ERDSLRANLLDNNNKL----DALRKLSD---GSSKSMDltkkaiHLsqselekyRKNNDDLQKEIDRI----KTEQAEQD 825
Cdd:pfam15921  378 QLQKLLADLHKREKELslekEQNKRLWDrdtGNSITID------HL--------RRELDDRNMEVQRLeallKAMKSECQ 443
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 398366259   826 DKQEQRGAITHGNFDAFHrmKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQ 880
Cdd:pfam15921  444 GQMERQMAAIQGKNESLE--KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
485-874 7.61e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  485 FERKSDREEKKPQSSKVDSSINKESpgtgikVSKKNFpvlrgLTVDSEEYGSSSYKDTSCQKGipknLFDDLNLNLQTL- 563
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKEL------IEKKDH-----LTKELEDIKMSLQRSMSTQKA----LEEDLQIATKTIc 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  564 ----RLEAQQKELETARH-----ISQLEKEV---QRLMVIKEASKDSNFQTARLKNLEIQKTFLEsrindlknllmvkLS 631
Cdd:pfam05483 328 qlteEKEAQMEELNKAKAahsfvVTEFEATTcslEELLRTEQQRLEKNEDQLKIITMELQKKSSE-------------LE 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  632 QASKLCDQITIQNNGLKTC-SEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELH------TYLNESSCYLGKLLK 704
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHdleiqlTAIKTSEEHYLKEVE 474
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  705 SYPTSarppssekdnqiYEKDSLNKIEKVINemhetvraKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSK 784
Cdd:pfam05483 475 DLKTE------------LEKEKLKNIELTAH--------CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  785 SMD-LTKKAIHLsQSELEKYRKNNDDLQKEIdRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRDS 863
Cdd:pfam05483 535 QIEnLEEKEMNL-RDELESVREEFIQKGDEV-KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
                         410
                  ....*....|.
gi 398366259  864 LKDELLALKKK 874
Cdd:pfam05483 613 LHQENKALKKK 623
Kelch_3 pfam13415
Galactose oxidase, central domain;
266-315 8.80e-06

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 43.43  E-value: 8.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366259  266 DNKLWVFGGETPK--TISNDTYRYDPAQSEWskvKTTGEKPPPIQEHASVVY 315
Cdd:pfam13415   1 GDKLYIFGGLGFDgqTRLNDLYVYDLDTNTW---TQIGDLPPPRSGHSATYI 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
560-882 3.86e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  560 LQTLRLEAQQKELEtarhISQLEKEVQRL-MVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCD 638
Cdd:TIGR04523 372 IEKLKKENQSYKQE----IKNLESQINDLeSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  639 QITIQNNGLKtcsehvTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELHTYLNEsscyLGKLlksyptsarppSSEKd 718
Cdd:TIGR04523 448 QDSVKELIIK------NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKKL-----------NEEK- 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  719 nqiyeKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANL--LDNNNKLDALRKLSDGSSKSMD---LTKKAI 793
Cdd:TIGR04523 506 -----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEelkQTQKSL 580
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  794 HLSQSELE----KYRKNNDDLQKEIDrIKTEQAEQDDKQeqrgaITHGNfdAFHRmKINNLKAELYMSKEnrdSLKDELL 869
Cdd:TIGR04523 581 KKKQEEKQelidQKEKEKKDLIKEIE-EKEKKISSLEKE-----LEKAK--KENE-KLSSIIKNIKSKKN---KLKQEVK 648
                         330
                  ....*....|...
gi 398366259  870 ALKKKLYTLEQKK 882
Cdd:TIGR04523 649 QIKETIKEIRNKW 661
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
566-879 3.92e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  566 EAQQKELEtaRHISQLEKEV-QRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQN 644
Cdd:TIGR04523  32 DTEEKQLE--KKLKTIKNELkNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  645 NGLKtcsehvTIKRDIIDLENKCDVLKRQ------NEILVNNMQKITPELHTYLNESSCYLGKLLKSYptsarppssEKD 718
Cdd:TIGR04523 110 SEIK------NDKEQKNKLEVELNKLEKQkkenkkNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL---------ENE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  719 NQIYEKDsLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsDGSSKSMDLTKKAIHLS-- 796
Cdd:TIGR04523 175 LNLLEKE-KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD--NIEKKQQEINEKTTEISnt 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  797 ---------------------QSELEKYRKNNDDLQKEIDRIKTE------QAEQDDKQEQRGAITHgnfdafHRMKINN 849
Cdd:TIGR04523 252 qtqlnqlkdeqnkikkqlsekQKELEQNNKKIKELEKQLNQLKSEisdlnnQKEQDWNKELKSELKN------QEKKLEE 325
                         330       340       350
                  ....*....|....*....|....*....|
gi 398366259  850 LKAELYMSKENRDSLKDELLALKKKLYTLE 879
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSE 355
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
559-882 5.32e-05

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.35  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   559 NLQTLRLEAQQKELETARH-ISQLEKEVQRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLC 637
Cdd:TIGR01612 1222 NLGKLFLEKIDEEKKKSEHmIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS 1301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   638 DqitIQNNGLKTcSEHVTIKRDIIDLenkcdvlKRQNEILVNNMQKITPELHTYLNESScylgkllksyptsarppssek 717
Cdd:TIGR01612 1302 D---IREKSLKI-IEDFSEESDINDI-------KKELQKNLLDAQKHNSDINLYLNEIA--------------------- 1349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   718 dnQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLS--------DGSSKSMDLT 789
Cdd:TIGR01612 1350 --NIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIEstlddkdiDECIKKIKEL 1427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   790 KKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRDSLKDELL 869
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAK 1507
                          330
                   ....*....|...
gi 398366259   870 ALKKKLYTLEQKK 882
Cdd:TIGR01612 1508 AIEKNKELFEQYK 1520
Kelch_3 pfam13415
Galactose oxidase, central domain;
151-205 6.15e-05

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 41.12  E-value: 6.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398366259  151 GNAYVVFGGDTHKlnkNGLLDDDLYLFNINSYKWTipqPIGRRPLGRYGHKISII 205
Cdd:pfam13415   1 GDKLYIFGGLGFD---GQTRLNDLYVYDLDTNTWT---QIGDLPPPRSGHSATYI 49
Kelch_6 pfam13964
Kelch motif;
258-297 8.71e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 40.78  E-value: 8.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 398366259  258 TNHTMVAYDNKLWVFGGET-PKTISNDTYRYDPAQSEWSKV 297
Cdd:pfam13964   3 TFHSVVSVGGYIYVFGGYTnASPALNKLEVYNPLTKSWEEL 43
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
571-831 1.07e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   571 ELETARHISQLEKEVQRLMVIKEASKDSNFQTARLK-NLEIQKTFLESRINDLKNLLMVkLSQAsklcdqitiqnnglKT 649
Cdd:pfam01576  337 EEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKaNLEKAKQALESENAELQAELRT-LQQA--------------KQ 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   650 CSEHVTIKRD--IIDLENKCDVLKRQNEILVNNMQKITPELH---TYLNESScylGKLLKSYPTSARPPSSEKDNQiyek 724
Cdd:pfam01576  402 DSEHKRKKLEgqLQELQARLSESERQRAELAEKLSKLQSELEsvsSLLNEAE---GKNIKLSKDVSSLESQLQDTQ---- 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   725 dslnkiekviNEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDAL-RKLSDGSSKSMDLTKKAIHLSQS--ELE 801
Cdd:pfam01576  475 ----------ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSDMKKKLEEDAGTleALE 544
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 398366259   802 KYRKNnddLQKEIDRI------KTEQAEQDDKQEQR 831
Cdd:pfam01576  545 EGKKR---LQRELEALtqqleeKAAAYDKLEKTKNR 577
Kelch_4 pfam13418
Galactose oxidase, central domain;
141-185 1.64e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.90  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 398366259  141 PRVGHASTICGNAYV-VFGGdthkLNKNGLLDDDLYLFNINSYKWT 185
Cdd:pfam13418   1 PRAYHTSTSIPDDTIyLFGG----EGEDGTLLSDLWVFDLSTNEWT 42
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
554-866 2.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 554 DDLNLNLQTLR---------LEAQQKELETARH-ISQLEKEVQRLM-VIKEASKDSNFQTARLKNLEIQKTFLESRINDL 622
Cdd:COG4372   41 DKLQEELEQLReeleqareeLEQLEEELEQARSeLEQLEEELEELNeQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 623 KNllmvKLSQASKLCDQITIQNNGLKtcSEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPElhtylnESSCYLGKL 702
Cdd:COG4372  121 QK----ERQDLEQQRKQLEAQIAELQ--SEIAEREEELKELEEQLESLQEELAALEQELQALSEA------EAEQALDEL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 703 LKSYPTSArPPSSEKDNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGS 782
Cdd:COG4372  189 LKEANRNA-EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 783 SKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRD 862
Cdd:COG4372  268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347

                 ....
gi 398366259 863 SLKD 866
Cdd:COG4372  348 VGLL 351
Kelch_3 pfam13415
Galactose oxidase, central domain;
213-265 2.44e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.58  E-value: 2.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398366259  213 KLYLFGGQVDE--TYFNDLVVFDLSSfrrpnshWEFlEPVGDLPPPLTNHTMVAY 265
Cdd:pfam13415   3 KLYIFGGLGFDgqTRLNDLYVYDLDT-------NTW-TQIGDLPPPRSGHSATYI 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
724-882 2.54e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   724 KDSLNKIEKVINEMHetvRAKEKLHLETQK------LNDERDSLRANLLdnNNKLDALRKlsdgsskSMDLTKKAIHLSQ 797
Cdd:TIGR02168  185 RENLDRLEDILNELE---RQLKSLERQAEKaerykeLKAELRELELALL--VLRLEELRE-------ELEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   798 SELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFDafHRMKINNLKAELYMSKENRDSLKDELLALKKKLYT 877
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEE---LQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                   ....*
gi 398366259   878 LEQKK 882
Cdd:TIGR02168  328 LESKL 332
PHA03098 PHA03098
kelch-like protein; Provisional
165-387 3.06e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 44.37  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 165 NKNGLLDDDLYLFNINSYKW-TIPQPIGRRPLgryghkISIIASNpmqTKLYLFGGQVDETYFNDLvvfdlssfrrpnSH 243
Cdd:PHA03098 304 NKNNLSVNSVVSYDTKTKSWnKVPELIYPRKN------PGVTVFN---NRIYVIGGIYNSISLNTV------------ES 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 244 WEFLEPVGDLPPPL----TNHTMVAYDNKLWVFGG-ETPKTISNDTYRYDPAQSEWSKVKTTgekPPPIQEHASVVYKHL 318
Cdd:PHA03098 363 WKPGESKWREEPPLifprYNPCVVNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGK 439
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366259 319 MCVLGGKDTHNAYS--NDVYFLNLLSLKWYKLPRMKegipQERSGHSLTLMkNEKLLIMGGDKTDYASPNI 387
Cdd:PHA03098 440 IYVIGGISYIDNIKvyNIVESYNPVTNKWTELSSLN----FPRINASLCIF-NNKIYVVGGDKYEYYINEI 505
PHA03098 PHA03098
kelch-like protein; Provisional
93-298 3.22e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 44.37  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  93 IVTNDNRIFVTGGLHDQSVYGDV--WQIAANAdgtsftskridiDQNTPP---PRVGHASTICGNAYVVFGGdthkLNKN 167
Cdd:PHA03098 338 VTVFNNRIYVIGGIYNSISLNTVesWKPGESK------------WREEPPlifPRYNPCVVNVNNLIYVIGG----ISKN 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 168 GLLDDDLYLFNINSYKWTIPQPIgrrplgRYGHKISIIASNpmQTKLYLFGGQvdeTYFNDLVVFD-LSSFRRPNSHWEF 246
Cdd:PHA03098 402 DELLKTVECFSLNTNKWSKGSPL------PISHYGGCAIYH--DGKIYVIGGI---SYIDNIKVYNiVESYNPVTNKWTE 470
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366259 247 LEPvgdLPPPLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVK 298
Cdd:PHA03098 471 LSS---LNFPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWTLFC 519
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
716-881 3.89e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 716 EKDNQIYE-KDSLNKIEKVINEMHETVRAKEKlhlETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:COG1579   14 ELDSELDRlEHRLKELPAELAELEDELAALEA---RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 795 LS--QSELEKYRKNNDDLQKEI----DRIKTEQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELymsKENRDSLKDEL 868
Cdd:COG1579   91 YEalQKEIESLKRRISDLEDEIlelmERIEELEEELAELEAELAELEA---------ELEEKKAEL---DEELAELEAEL 158
                        170
                 ....*....|...
gi 398366259 869 LALKKKLYTLEQK 881
Cdd:COG1579  159 EELEAEREELAAK 171
Kelch_6 pfam13964
Kelch motif;
310-354 4.87e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.86  E-value: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 398366259  310 HASVVYKHLMCVLGGKDTHNAYSNDVYFLNLLSLKWYKLPRMKEG 354
Cdd:pfam13964   5 HSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTP 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
254-290 6.88e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 37.93  E-value: 6.88e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 398366259  254 PPPLTNHTMVAYDNKLWVFGGETP--KTISNDTYRYDPA 290
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTGgeGQPSDDVYVLSLP 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
729-871 7.54e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  729 KIEKVINEMHETVRAKEKLHLETQKLNDERDSLRAnlldnnnKLDALRKLSDGSSKSMDL--TKKAIHLSQSELEKYRKN 806
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQE-------RREALQRLAEYSWDEIDVasAEREIAELEAELERLDAS 683
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259  807 NDDLQKEIDRIKTEQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELYMSKENRDSLKDELLAL 871
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKG---------EIGRLEKELEQAEEELDELQDRLEAA 739
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
714-882 1.25e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 714 SSEKDNQIYEKdslnkiekvINEMHETVRAKEKLHLETQKLNDER---DSLRANLLDNNNKLDALRKLSDGSSKSMDLTK 790
Cdd:COG1340  131 SPEEEKELVEK---------IKELEKELEKAKKALEKNEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 791 KaihlsqsELEKYRKNNDDLQKEIDRIKtEQAEQddkqeqrgaithgnfdafHRMKINNLKAELymsKENRDSLKdellA 870
Cdd:COG1340  202 K-------EADELRKEADELHKEIVEAQ-EKADE------------------LHEEIIELQKEL---RELRKELK----K 248
                        170
                 ....*....|..
gi 398366259 871 LKKKLYTLEQKK 882
Cdd:COG1340  249 LRKKQRALKREK 260
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
727-882 1.37e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.93  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   727 LNKIEKVINEMHET-VRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKsmdltkkaihLSQSELEKYRK 805
Cdd:smart00787 142 LEGLKEGLDENLEGlKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELED----------CDPTELDRAKE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259   806 NNDDLQKEIDRIKTEQAE-QDDKQEQRGAITHGNfdafhrMKINNLKAELYMS----KENRDSLKDELLALKKKLYTLEQ 880
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEElEEELQELESKIEDLT------NKKSELNTEIAEAekklEQCRGFTFKEIEKLKEQLKLLQS 285

                   ..
gi 398366259   881 KK 882
Cdd:smart00787 286 LT 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
557-880 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 557 NLNLQTLRLEAQQKELETarHISQLEKEVQRLmviKEASKDSNFQTARLKNLEiQKTFLESRINDLKNLLMVKLSQASKL 636
Cdd:PRK03918 242 ELEKELESLEGSKRKLEE--KIRELEERIEEL---KKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKR 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 637 CDQITIQNNGlktcsehvtIKRDIIDLENKcdvLKRQNEIlvnnmQKITPELHTYLNEsscyLGKLLKSYPTsARPPSSE 716
Cdd:PRK03918 316 LSRLEEEING---------IEERIKELEEK---EERLEEL-----KKKLKELEKRLEE----LEERHELYEE-AKAKKEE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 717 KdNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsdgssksmdlTKKAIHLS 796
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----------AKGKCPVC 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 797 QSEL-EKYRKN-NDDLQKEIDRIKTEQAEQDDKQEQrgaithgnfdafhrMKINNLKAELYMSKENR----DSLKDELLA 870
Cdd:PRK03918 442 GRELtEEHRKElLEEYTAELKRIEKELKEIEEKERK--------------LRKELRELEKVLKKESEliklKELAEQLKE 507
                        330
                 ....*....|..
gi 398366259 871 LKKKL--YTLEQ 880
Cdd:PRK03918 508 LEEKLkkYNLEE 519
PHA03098 PHA03098
kelch-like protein; Provisional
206-377 1.67e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 42.06  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 206 ASNPMQTKLYLFGGQVDETYFNDLVV-FDLSSFRrpnshwefLEPVGDLPPPLTNHTMVAYDNKLWVFGGETPKTISNDT 284
Cdd:PHA03098 289 GSVVLNNVIYFIGGMNKNNLSVNSVVsYDTKTKS--------WNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTV 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 285 YRYDPAQSEWSkvkttgEKPPPIQ---EHASVVYKHLMCVLGGKDTHNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSG 361
Cdd:PHA03098 361 ESWKPGESKWR------EEPPLIFpryNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL----PISHYG 430
                        170
                 ....*....|....*.
gi 398366259 362 HSlTLMKNEKLLIMGG 377
Cdd:PHA03098 431 GC-AIYHDGKIYVIGG 445
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
743-882 2.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 743 AKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQA 822
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366259 823 EQDDKQEQ--RGAITHGNFDA----FHRMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQKK 882
Cdd:COG4942  101 AQKEELAEllRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
588-881 2.27e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 588 LMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQNNglktcsehvTIKRDIIDLEnkc 667
Cdd:COG5185  228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN---------NLIKQFENTK--- 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 668 dvlkrqnEILVNNMQKITPELHTylNESSCYLGK--LLKSYPTSARPPSSEKDNQIYE----KDSLNKIEKVINEMHETV 741
Cdd:COG5185  296 -------EKIAEYTKSIDIKKAT--ESLEEQLAAaeAEQELEESKRETETGIQNLTAEieqgQESLTENLEAIKEEIENI 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 742 RAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAiHLSQSE-----LEKYRKNNDDLQKEIDR 816
Cdd:COG5185  367 VGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA-ADRQIEelqrqIEQATSSNEEVSKLLNE 445
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 817 IKTEQAEQDDKQEqrgAITHGNFDAFHRMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQK 881
Cdd:COG5185  446 LISELNKVMREAD---EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAK 507
PHA03098 PHA03098
kelch-like protein; Provisional
56-233 2.53e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 41.29  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259  56 STALPWSPeskntGKYIWNRvkLKNSPFPRYrhsSSFIVTNDNRIFVTGGLHDQSVYGDVWQIaanadgTSFTSKRIDID 135
Cdd:PHA03098 358 NTVESWKP-----GESKWRE--EPPLIFPRY---NPCVVNVNNLIYVIGGISKNDELLKTVEC------FSLNTNKWSKG 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 136 QNTPPPRVGHASTICGNAYVVFGGDTHKLNKNGLldDDLYLFNINSYKWTIPQPIgRRPlgRYGHKISIIasnpmQTKLY 215
Cdd:PHA03098 422 SPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVY--NIVESYNPVTNKWTELSSL-NFP--RINASLCIF-----NNKIY 491
                        170
                 ....*....|....*...
gi 398366259 216 LFGGQVDETYFNDLVVFD 233
Cdd:PHA03098 492 VVGGDKYEYYINEIEVYD 509
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
564-882 4.57e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 564 RLEAQQKELETARhisQLEKEVQRLMV-------------IKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMvKL 630
Cdd:PRK03918 356 ELEERHELYEEAK---AKKEELERLKKrltgltpeklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-EL 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 631 SQASKLCD----QITIQNNGLKTCSEHVTIKR------DIIDLENKCDVLKRQNEILVNNMQKITPELHTY--LNEsscy 698
Cdd:PRK03918 432 KKAKGKCPvcgrELTEEHRKELLEEYTAELKRiekelkEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKE---- 507
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 699 LGKLLKSYPTSarppSSEKDNQIYEK----------------DSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLR 762
Cdd:PRK03918 508 LEEKLKKYNLE----ELEKKAEEYEKlkekliklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 763 ANLLDN-NNKLDALRKLSD------GSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKT--EQAEQDDKQEqrga 833
Cdd:PRK03918 584 FESVEElEERLKELEPFYNeylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKelEELEKKYSEE---- 659
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366259 834 iTHGNFDAFH---RMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQKK 882
Cdd:PRK03918 660 -EYEELREEYlelSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
565-824 4.77e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 565 LEAQQKELETAR--HISQLEKEVQRLMVIKEASKDSNFQTARLKNlEIQKTFleSRINDLKNllmvKLSQASKLCDQITI 642
Cdd:COG1340   34 LNEELKELAEKRdeLNAQVKELREEAQELREKRDELNEKVKELKE-ERDELN--EKLNELRE----ELDELRKELAELNK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 643 QNNGLKTcsehvtIKRDIIDLENKCD--VLKRQNEI-LVNNMQKITPELHtylnesscylgkllksyptsARPPSSEKDN 719
Cdd:COG1340  107 AGGSIDK------LRKEIERLEWRQQteVLSPEEEKeLVEKIKELEKELE--------------------KAKKALEKNE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 720 QIYE-KDSLNKIEKVINEMHETVRAK----EKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:COG1340  161 KLKElRAELKELRKEAEEIHKKIKELaeeaQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 398366259 795 LSQSELEKYRKNNDDLQKEIDR-IKTEQAEQ 824
Cdd:COG1340  241 ELRKELKKLRKKQRALKREKEKeELEEKAEE 271
Kelch_4 pfam13418
Galactose oxidase, central domain;
196-255 6.32e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 35.67  E-value: 6.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366259  196 GRYGHKISIIASNpmqtKLYLFGGQ-VDETYFNDLVVFDLSSfrrpNsHWeflEPVGDLPP 255
Cdd:pfam13418   1 PRAYHTSTSIPDD----TIYLFGGEgEDGTLLSDLWVFDLST----N-EW---TRLGSLPS 49
Kelch_3 pfam13415
Galactose oxidase, central domain;
316-366 6.74e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 35.34  E-value: 6.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366259  316 KHLMCVLGGKDT-HNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTL 366
Cdd:pfam13415   1 GDKLYIFGGLGFdGQTRLNDLYVYDLDTNTWTQIGDL----PPPRSGHSATY 48
 
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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