|
Name |
Accession |
Description |
Interval |
E-value |
| APC_basic super family |
cl25885 |
APC basic domain; This region of the APC family of proteins is known as the basic domain. It ... |
1869-2137 |
4.53e-63 |
|
APC basic domain; This region of the APC family of proteins is known as the basic domain. It contains a high proportion of positively charged amino acids and interacts with microtubules.
The actual alignment was detected with superfamily member pfam05956:
Pssm-ID: 428690 [Multi-domain] Cd Length: 336 Bit Score: 219.36 E-value: 4.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1869 VLRGRTVIYVPAKeKESSTKllQNQAPHiKDPTKVATAV--------RSRSLHRLGKSSDLgVEMTLPKRSATPPARISN 1940
Cdd:pfam05956 2 VFRGRTVIYMPGV-KESQPS--TSPPPK-KTPPKTDAPAknpnlgqqRSRSLHRLGKPSEL-ADLSPPKRSATPPARISK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1941 ASSSSSSRNSTPSRKAQAPVPSPIS---------KRSKNTQVL-------------PGNKTQKSPVRIPFMKKPT--PRC 1996
Cdd:pfam05956 77 APSSGSSRDSTPSRPPQKKLTSPSQspgrlpgsgGRNKLSPLPktksparastkksGSHKTQKSPVRIPFMQTPTkqTGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1997 PPGPSPLAIEPVSPLQSP----SRRPQGSRLNQVK-------NSESEKSGMLRQLTFIKESSGSMRRQHSDLSVSR---- 2061
Cdd:pfam05956 157 PRNPSPLVTNQPEPRSESaskgLRSLPGKRLDLVRmssarssGSESDRSGFLRQLTFIKESPSLLLRRRLELSASEslsp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2062 --QHRIPPPKNSALPAVFLCSSRCEELKVHKQ--PKPKVTASPNC-------PPRRTSSESPSRLPVRNLPPAPEPFKRY 2130
Cdd:pfam05956 237 ssQPASPRRSRPGLPAVFLCSSRCQELKGWRKqpPNPNSRAEPSDrpltrrrPPRRTSSESPSRLPVRNGTWKRETFKRY 316
|
....*..
gi 847093691 2131 SSSPHIN 2137
Cdd:pfam05956 317 SSLPHIN 323
|
|
| APC_rep |
pfam18797 |
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo ... |
328-400 |
2.36e-37 |
|
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo repeat and uses its highly conserved surface groove to recognize the APC-binding region (ABR) of Asef. This entry represents a single repeat unit of the Armadillo region.
:
Pssm-ID: 465870 Cd Length: 74 Bit Score: 135.37 E-value: 2.36e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 328 SQPDEGQAKKEMRVLHILEQIRSYTETCCDWMLEHER-VGNMHECNPVPVEPQICQASCAIMKLSFDEEYRRAM 400
Cdd:pfam18797 1 SQPDDKRGRREMRVLHLLEQIRAYCETCWDWQESHSRgPEGDSNPMPSPIEHQICPAICALMKLSFDEEHRHAM 74
|
|
| Arm_APC_u3 super family |
cl25003 |
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately ... |
666-940 |
3.67e-33 |
|
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately downstream of the armadillo fold before the beta-catenin binding motifs, APC_crr, pfam05923, on APC or adenomatous polyposis coli proteins in higher eukaryotes. The function is not known.
The actual alignment was detected with superfamily member pfam16629:
Pssm-ID: 435476 Cd Length: 293 Bit Score: 131.25 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 666 HRPVKYKDASVISPGSCMPSLYMRKQKALEAELDAKHLAETID-------KQGLKSQPvkgplRHIESLVKDYASDSGCF 738
Cdd:pfam16629 1 NRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDnidnlspKASHRNKQ-----RHKQNVYSEYVLDSGRH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 739 DDDDIPNTSISaeTGNSSVLSMYLNSSYTQGQ-------NIPRTGSLK-RAGELEKVDSCKNEIRKPHEYISSADKLPTK 810
Cdd:pfam16629 76 DDSVCRSDNFN--TGNVTVLSPYLNTTVLPSSssrdsrgNAESSRSEKdRSLDRERGAGLSNFHPATENSGNSSKRIGMQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 811 IPSAISKIDRLVEDVSTMHTSSDDSFSLSSEdhciDWPCGSDELHEAR----AHSCSPCRLSDKSgllrrDNISRAQALL 886
Cdd:pfam16629 154 ISTTAAQIAKVMEEVSSMHISQEDRSSGSTS----DMHCMQDDRNSIRrsstAHPHSNVYSFNKS-----ESSNRPCPMP 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 847093691 887 RLKTAYTSLSNDSLNSGSTSDGYCPKEHMKPCSRSSLIDYKDELQRYQKRPSRL 940
Cdd:pfam16629 225 YMKMEYKRASNDSLNSVSSSDGYGKRGQMKPSVESYSEDDEGKFCSYGKYPADL 278
|
|
| APC_N_CC |
pfam16689 |
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil ... |
14-65 |
1.03e-16 |
|
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil dimerization domain of the adenomatosis polyposis coli (APC) tumour-repressor proteins. It plays a key role in the regulation of cellular levels of the oncogene product beta-catenin. Coiled-coil regions are binding repeats that in this case bind to the armadillo repeat region of beta-catenin.
:
Pssm-ID: 435517 Cd Length: 52 Bit Score: 75.80 E-value: 1.03e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 847093691 14 ASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKL 65
Cdd:pfam16689 1 ASYDQLLRQVEALKLENTTLRQELRDNSSHLSKLETEASNMKEVLKHLQGSI 52
|
|
| Suppressor_APC |
pfam11414 |
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has ... |
109-182 |
1.21e-15 |
|
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has a nuclear export activity as well as many different intracellular functions. The structure consists of three alpha-helices forming two separate antiparallel coiled coils.
:
Pssm-ID: 463275 Cd Length: 82 Bit Score: 73.83 E-value: 1.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847093691 109 LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPHAET-FSLQIDLIRQQLEFESDHLHCVLEERFGT 182
Cdd:pfam11414 7 RMKQLEQEKDVLLQGLEMVERARDWYQQQLQEVQERQKYLGANGTyFDYGSDAQQERLEFLLARIQEVNRCLGGL 81
|
|
| SMC_prok_B super family |
cl37069 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-415 |
3.00e-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]
The actual alignment was detected with superfamily member TIGR02168:
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 25 DLKKENSHL--RRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPMQLEIPQKRARDE 102
Cdd:TIGR02168 665 SAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELE----------ELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 103 srtsellMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEEL---------------PHAETFSLQIDLIRQQLEF 167
Cdd:TIGR02168 735 -------LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaeaeaeieeleAQIEQLKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 168 ESDHLHcVLEERFGTADEMVQRAQIRASHLEQIEQQLEEmQSKEVKEHQVIEEKSMD----LAEKINTEAVAPPDDSSGQ 243
Cdd:TIGR02168 808 LRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEeleeLIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 244 QEskvevvfwlLSMLANRDKDDMSRTLLAMSSsqdscqamrrsgclplliqilheaerdtkapESSAFKDARMRANAALH 323
Cdd:TIGR02168 886 EE---------ALALLRSELEELSEELRELES-------------------------------KRSELRRELEELREKLA 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 324 NVifsqpDEGQAKKEMRVLHILEQIRSytetccDWMLEHERVGNMHecNPVPVEPQICQAScaIMKLsfdeeyRRAMNEL 403
Cdd:TIGR02168 926 QL-----ELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALE--NKIEDDEEEARRR--LKRL------ENKIKEL 984
|
410
....*....|....
gi 847093691 404 GG--LQAIAELLEV 415
Cdd:TIGR02168 985 GPvnLAAIEEYEEL 998
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
584-623 |
7.37e-07 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
:
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 47.45 E-value: 7.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 847093691 584 DDYRQILRDHNCLQTLLQHLRSHSLTIVSNACGTLWNLSA 623
Cdd:pfam00514 2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| SAMP |
pfam05924 |
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1364-1384 |
2.18e-04 |
|
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). This motif binds axin.
:
Pssm-ID: 461782 Cd Length: 22 Bit Score: 40.27 E-value: 2.18e-04
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
630-665 |
1.55e-03 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
:
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 38.20 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*.
gi 847093691 630 ELLWDLGAISMLRNLIHSKHKMIAMGSAAALRNLLA 665
Cdd:pfam00514 6 QAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| APC_r |
pfam05923 |
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1434-1456 |
3.20e-03 |
|
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). In the human protein many cancer-linked SNPs are found near the first three occurrences of the motif. These repeats bind beta-catenin.
:
Pssm-ID: 461781 Cd Length: 24 Bit Score: 36.97 E-value: 3.20e-03
|
| EB1_binding super family |
cl05480 |
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the ... |
2263-2284 |
5.28e-03 |
|
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the microtubule-associating protein EB-1. At the C-terminus of the alignment is also a pfam00595 binding domain. A short motif in the middle of the region appears to be found in the APC2 proteins.
The actual alignment was detected with superfamily member pfam05937:
Pssm-ID: 399141 Cd Length: 174 Bit Score: 39.98 E-value: 5.28e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| APC_basic |
pfam05956 |
APC basic domain; This region of the APC family of proteins is known as the basic domain. It ... |
1869-2137 |
4.53e-63 |
|
APC basic domain; This region of the APC family of proteins is known as the basic domain. It contains a high proportion of positively charged amino acids and interacts with microtubules.
Pssm-ID: 428690 [Multi-domain] Cd Length: 336 Bit Score: 219.36 E-value: 4.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1869 VLRGRTVIYVPAKeKESSTKllQNQAPHiKDPTKVATAV--------RSRSLHRLGKSSDLgVEMTLPKRSATPPARISN 1940
Cdd:pfam05956 2 VFRGRTVIYMPGV-KESQPS--TSPPPK-KTPPKTDAPAknpnlgqqRSRSLHRLGKPSEL-ADLSPPKRSATPPARISK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1941 ASSSSSSRNSTPSRKAQAPVPSPIS---------KRSKNTQVL-------------PGNKTQKSPVRIPFMKKPT--PRC 1996
Cdd:pfam05956 77 APSSGSSRDSTPSRPPQKKLTSPSQspgrlpgsgGRNKLSPLPktksparastkksGSHKTQKSPVRIPFMQTPTkqTGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1997 PPGPSPLAIEPVSPLQSP----SRRPQGSRLNQVK-------NSESEKSGMLRQLTFIKESSGSMRRQHSDLSVSR---- 2061
Cdd:pfam05956 157 PRNPSPLVTNQPEPRSESaskgLRSLPGKRLDLVRmssarssGSESDRSGFLRQLTFIKESPSLLLRRRLELSASEslsp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2062 --QHRIPPPKNSALPAVFLCSSRCEELKVHKQ--PKPKVTASPNC-------PPRRTSSESPSRLPVRNLPPAPEPFKRY 2130
Cdd:pfam05956 237 ssQPASPRRSRPGLPAVFLCSSRCQELKGWRKqpPNPNSRAEPSDrpltrrrPPRRTSSESPSRLPVRNGTWKRETFKRY 316
|
....*..
gi 847093691 2131 SSSPHIN 2137
Cdd:pfam05956 317 SSLPHIN 323
|
|
| APC_rep |
pfam18797 |
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo ... |
328-400 |
2.36e-37 |
|
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo repeat and uses its highly conserved surface groove to recognize the APC-binding region (ABR) of Asef. This entry represents a single repeat unit of the Armadillo region.
Pssm-ID: 465870 Cd Length: 74 Bit Score: 135.37 E-value: 2.36e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 328 SQPDEGQAKKEMRVLHILEQIRSYTETCCDWMLEHER-VGNMHECNPVPVEPQICQASCAIMKLSFDEEYRRAM 400
Cdd:pfam18797 1 SQPDDKRGRREMRVLHLLEQIRAYCETCWDWQESHSRgPEGDSNPMPSPIEHQICPAICALMKLSFDEEHRHAM 74
|
|
| Arm_APC_u3 |
pfam16629 |
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately ... |
666-940 |
3.67e-33 |
|
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately downstream of the armadillo fold before the beta-catenin binding motifs, APC_crr, pfam05923, on APC or adenomatous polyposis coli proteins in higher eukaryotes. The function is not known.
Pssm-ID: 435476 Cd Length: 293 Bit Score: 131.25 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 666 HRPVKYKDASVISPGSCMPSLYMRKQKALEAELDAKHLAETID-------KQGLKSQPvkgplRHIESLVKDYASDSGCF 738
Cdd:pfam16629 1 NRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDnidnlspKASHRNKQ-----RHKQNVYSEYVLDSGRH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 739 DDDDIPNTSISaeTGNSSVLSMYLNSSYTQGQ-------NIPRTGSLK-RAGELEKVDSCKNEIRKPHEYISSADKLPTK 810
Cdd:pfam16629 76 DDSVCRSDNFN--TGNVTVLSPYLNTTVLPSSssrdsrgNAESSRSEKdRSLDRERGAGLSNFHPATENSGNSSKRIGMQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 811 IPSAISKIDRLVEDVSTMHTSSDDSFSLSSEdhciDWPCGSDELHEAR----AHSCSPCRLSDKSgllrrDNISRAQALL 886
Cdd:pfam16629 154 ISTTAAQIAKVMEEVSSMHISQEDRSSGSTS----DMHCMQDDRNSIRrsstAHPHSNVYSFNKS-----ESSNRPCPMP 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 847093691 887 RLKTAYTSLSNDSLNSGSTSDGYCPKEHMKPCSRSSLIDYKDELQRYQKRPSRL 940
Cdd:pfam16629 225 YMKMEYKRASNDSLNSVSSSDGYGKRGQMKPSVESYSEDDEGKFCSYGKYPADL 278
|
|
| APC_N_CC |
pfam16689 |
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil ... |
14-65 |
1.03e-16 |
|
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil dimerization domain of the adenomatosis polyposis coli (APC) tumour-repressor proteins. It plays a key role in the regulation of cellular levels of the oncogene product beta-catenin. Coiled-coil regions are binding repeats that in this case bind to the armadillo repeat region of beta-catenin.
Pssm-ID: 435517 Cd Length: 52 Bit Score: 75.80 E-value: 1.03e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 847093691 14 ASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKL 65
Cdd:pfam16689 1 ASYDQLLRQVEALKLENTTLRQELRDNSSHLSKLETEASNMKEVLKHLQGSI 52
|
|
| Suppressor_APC |
pfam11414 |
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has ... |
109-182 |
1.21e-15 |
|
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has a nuclear export activity as well as many different intracellular functions. The structure consists of three alpha-helices forming two separate antiparallel coiled coils.
Pssm-ID: 463275 Cd Length: 82 Bit Score: 73.83 E-value: 1.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847093691 109 LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPHAET-FSLQIDLIRQQLEFESDHLHCVLEERFGT 182
Cdd:pfam11414 7 RMKQLEQEKDVLLQGLEMVERARDWYQQQLQEVQERQKYLGANGTyFDYGSDAQQERLEFLLARIQEVNRCLGGL 81
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-415 |
3.00e-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: 59.30 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 25 DLKKENSHL--RRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPMQLEIPQKRARDE 102
Cdd:TIGR02168 665 SAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELE----------ELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 103 srtsellMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEEL---------------PHAETFSLQIDLIRQQLEF 167
Cdd:TIGR02168 735 -------LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaeaeaeieeleAQIEQLKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 168 ESDHLHcVLEERFGTADEMVQRAQIRASHLEQIEQQLEEmQSKEVKEHQVIEEKSMD----LAEKINTEAVAPPDDSSGQ 243
Cdd:TIGR02168 808 LRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEeleeLIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 244 QEskvevvfwlLSMLANRDKDDMSRTLLAMSSsqdscqamrrsgclplliqilheaerdtkapESSAFKDARMRANAALH 323
Cdd:TIGR02168 886 EE---------ALALLRSELEELSEELRELES-------------------------------KRSELRRELEELREKLA 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 324 NVifsqpDEGQAKKEMRVLHILEQIRSytetccDWMLEHERVGNMHecNPVPVEPQICQAScaIMKLsfdeeyRRAMNEL 403
Cdd:TIGR02168 926 QL-----ELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALE--NKIEDDEEEARRR--LKRL------ENKIKEL 984
|
410
....*....|....
gi 847093691 404 GG--LQAIAELLEV 415
Cdd:TIGR02168 985 GPvnLAAIEEYEEL 998
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1956-2293 |
4.61e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1956 AQAPVPSPISKRSKNTQVLPGNKTQKSPV--RIPFMKKPTPRCPPGPSPLAIEPVSP-LQSPSRRPQGSRLNQVKNsese 2032
Cdd:PHA03247 2456 ARTILGAPFSLSLLLGELFPGAPVYRRPAeaRFPFAAGAAPDPGGGGPPDPDAPPAPsRLAPAILPDEPVGEPVHP---- 2531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2033 ksgmlRQLTFIKessgSMRRQHSD-------------LSVSRQHRIPPPKNSALPAVFLCSSRCEELKVHKQP-KPKVTA 2098
Cdd:PHA03247 2532 -----RMLTWIR----GLEELASDdagdpppplppaaPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSaRPRAPV 2602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2099 SPNCPPRRTSSESPsrLPVRNLPPAPEPFKRYSSSPHINLPGPRGECRKDQNASRAEEARVSRPHTALSQDRAT------ 2172
Cdd:PHA03247 2603 DDRGDPRGPAPPSP--LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAqasspp 2680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2173 --WRR--IRD------------------EDIPHILRSTLPACALPLTDDVSEPRRKTSDAVVQTEDIAVTKTNSSTSPTL 2230
Cdd:PHA03247 2681 qrPRRraARPtvgsltsladpppppptpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847093691 2231 ESSSMGSRNRPGLASSLLPELGKSALAVVNLPTSRHSSPSRAARVTPFNYVPSPILTVTEEAA 2293
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS 2823
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
584-623 |
7.37e-07 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 47.45 E-value: 7.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 847093691 584 DDYRQILRDHNCLQTLLQHLRSHSLTIVSNACGTLWNLSA 623
Cdd:pfam00514 2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| ARM |
smart00185 |
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ... |
583-623 |
1.14e-06 |
|
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.
Pssm-ID: 214547 [Multi-domain] Cd Length: 41 Bit Score: 47.04 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 847093691 583 RDDYRQILRDHNCLQTLLQHLRSHSLTIVSNACGTLWNLSA 623
Cdd:smart00185 1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-272 |
2.88e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 6 RVGMVGAAAS--YDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFK 83
Cdd:COG4372 21 KTGILIAALSeqLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE----------ELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 84 DISATPMQLEIPQKRARDESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELpHAETFSLQIDLIRQ 163
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL-EEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 164 QLEFESDHLHCVLEErfgtADEMVQRAQIRASHLEQI-EQQLEEMQSKEVKEHQVIEEKSMDLAEKINTEAVAPPDDSSG 242
Cdd:COG4372 170 EQELQALSEAEAEQA----LDELLKEANRNAEKEEELaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270
....*....|....*....|....*....|
gi 847093691 243 QQESKVEVVFWLLSMLANRDKDDMSRTLLA 272
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEE 275
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-207 |
9.52e-05 |
|
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: 47.81 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 32 HLRRELKDNSSQLNRLEHDTSDMKEvlkHLQVKLEHDVGGGAGHAEMLDQFKDISAtpmQLEIPQKRAR---DESRTSEL 108
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVSSLTA---QLESTKEMLRkvvEELTAKKM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 109 LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKR----LEELPHaetfslqidlirqqLEFESDHLHCVLEERFGTAD 184
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlkLQELQH--------------LKNEGDHLRNVQTECEALKL 555
|
170 180
....*....|....*....|...
gi 847093691 185 EMVQRAQIrashLEQIEQQLEEM 207
Cdd:pfam15921 556 QMAEKDKV----IEILRQQIENM 574
|
|
| SAMP |
pfam05924 |
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1364-1384 |
2.18e-04 |
|
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). This motif binds axin.
Pssm-ID: 461782 Cd Length: 22 Bit Score: 40.27 E-value: 2.18e-04
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-228 |
8.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 17 DQLVRQVEDLKK-ENSH-----LRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPM 90
Cdd:PRK03918 148 EKVVRQILGLDDyENAYknlgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE----------EVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 91 QLEipQKRARDESRTSEL-----LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEEL-----------PHAETF 154
Cdd:PRK03918 218 ELR--EELEKLEKEVKELeelkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkelkEKAEEY 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 155 SLQIDLIRQQLEFESDhlhcvLEERFGTADEMVQRAQIRASHLEQIEQQLEEMQSKEVKehqvIEEKSMDLAEK 228
Cdd:PRK03918 296 IKLSEFYEEYLDELRE-----IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEER 360
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
630-665 |
1.55e-03 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 38.20 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*.
gi 847093691 630 ELLWDLGAISMLRNLIHSKHKMIAMGSAAALRNLLA 665
Cdd:pfam00514 6 QAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| APC_r |
pfam05923 |
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1434-1456 |
3.20e-03 |
|
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). In the human protein many cancer-linked SNPs are found near the first three occurrences of the motif. These repeats bind beta-catenin.
Pssm-ID: 461781 Cd Length: 24 Bit Score: 36.97 E-value: 3.20e-03
|
| EB1_binding |
pfam05937 |
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the ... |
2263-2284 |
5.28e-03 |
|
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the microtubule-associating protein EB-1. At the C-terminus of the alignment is also a pfam00595 binding domain. A short motif in the middle of the region appears to be found in the APC2 proteins.
Pssm-ID: 399141 Cd Length: 174 Bit Score: 39.98 E-value: 5.28e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| APC_basic |
pfam05956 |
APC basic domain; This region of the APC family of proteins is known as the basic domain. It ... |
1869-2137 |
4.53e-63 |
|
APC basic domain; This region of the APC family of proteins is known as the basic domain. It contains a high proportion of positively charged amino acids and interacts with microtubules.
Pssm-ID: 428690 [Multi-domain] Cd Length: 336 Bit Score: 219.36 E-value: 4.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1869 VLRGRTVIYVPAKeKESSTKllQNQAPHiKDPTKVATAV--------RSRSLHRLGKSSDLgVEMTLPKRSATPPARISN 1940
Cdd:pfam05956 2 VFRGRTVIYMPGV-KESQPS--TSPPPK-KTPPKTDAPAknpnlgqqRSRSLHRLGKPSEL-ADLSPPKRSATPPARISK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1941 ASSSSSSRNSTPSRKAQAPVPSPIS---------KRSKNTQVL-------------PGNKTQKSPVRIPFMKKPT--PRC 1996
Cdd:pfam05956 77 APSSGSSRDSTPSRPPQKKLTSPSQspgrlpgsgGRNKLSPLPktksparastkksGSHKTQKSPVRIPFMQTPTkqTGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1997 PPGPSPLAIEPVSPLQSP----SRRPQGSRLNQVK-------NSESEKSGMLRQLTFIKESSGSMRRQHSDLSVSR---- 2061
Cdd:pfam05956 157 PRNPSPLVTNQPEPRSESaskgLRSLPGKRLDLVRmssarssGSESDRSGFLRQLTFIKESPSLLLRRRLELSASEslsp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2062 --QHRIPPPKNSALPAVFLCSSRCEELKVHKQ--PKPKVTASPNC-------PPRRTSSESPSRLPVRNLPPAPEPFKRY 2130
Cdd:pfam05956 237 ssQPASPRRSRPGLPAVFLCSSRCQELKGWRKqpPNPNSRAEPSDrpltrrrPPRRTSSESPSRLPVRNGTWKRETFKRY 316
|
....*..
gi 847093691 2131 SSSPHIN 2137
Cdd:pfam05956 317 SSLPHIN 323
|
|
| APC_rep |
pfam18797 |
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo ... |
328-400 |
2.36e-37 |
|
Adenomatous polyposis coli (APC) repeat; Adenomatous polyposis coli contains an armadillo repeat and uses its highly conserved surface groove to recognize the APC-binding region (ABR) of Asef. This entry represents a single repeat unit of the Armadillo region.
Pssm-ID: 465870 Cd Length: 74 Bit Score: 135.37 E-value: 2.36e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 328 SQPDEGQAKKEMRVLHILEQIRSYTETCCDWMLEHER-VGNMHECNPVPVEPQICQASCAIMKLSFDEEYRRAM 400
Cdd:pfam18797 1 SQPDDKRGRREMRVLHLLEQIRAYCETCWDWQESHSRgPEGDSNPMPSPIEHQICPAICALMKLSFDEEHRHAM 74
|
|
| Arm_APC_u3 |
pfam16629 |
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately ... |
666-940 |
3.67e-33 |
|
Armadillo-associated region on APC; Arm_APC_u3 is a semi-unstructured region lying immediately downstream of the armadillo fold before the beta-catenin binding motifs, APC_crr, pfam05923, on APC or adenomatous polyposis coli proteins in higher eukaryotes. The function is not known.
Pssm-ID: 435476 Cd Length: 293 Bit Score: 131.25 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 666 HRPVKYKDASVISPGSCMPSLYMRKQKALEAELDAKHLAETID-------KQGLKSQPvkgplRHIESLVKDYASDSGCF 738
Cdd:pfam16629 1 NRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDnidnlspKASHRNKQ-----RHKQNVYSEYVLDSGRH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 739 DDDDIPNTSISaeTGNSSVLSMYLNSSYTQGQ-------NIPRTGSLK-RAGELEKVDSCKNEIRKPHEYISSADKLPTK 810
Cdd:pfam16629 76 DDSVCRSDNFN--TGNVTVLSPYLNTTVLPSSssrdsrgNAESSRSEKdRSLDRERGAGLSNFHPATENSGNSSKRIGMQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 811 IPSAISKIDRLVEDVSTMHTSSDDSFSLSSEdhciDWPCGSDELHEAR----AHSCSPCRLSDKSgllrrDNISRAQALL 886
Cdd:pfam16629 154 ISTTAAQIAKVMEEVSSMHISQEDRSSGSTS----DMHCMQDDRNSIRrsstAHPHSNVYSFNKS-----ESSNRPCPMP 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 847093691 887 RLKTAYTSLSNDSLNSGSTSDGYCPKEHMKPCSRSSLIDYKDELQRYQKRPSRL 940
Cdd:pfam16629 225 YMKMEYKRASNDSLNSVSSSDGYGKRGQMKPSVESYSEDDEGKFCSYGKYPADL 278
|
|
| APC_N_CC |
pfam16689 |
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil ... |
14-65 |
1.03e-16 |
|
Coiled-coil N-terminus of APC, dimerization domain; APC_N_CC is the N-terminal, coiled-coil dimerization domain of the adenomatosis polyposis coli (APC) tumour-repressor proteins. It plays a key role in the regulation of cellular levels of the oncogene product beta-catenin. Coiled-coil regions are binding repeats that in this case bind to the armadillo repeat region of beta-catenin.
Pssm-ID: 435517 Cd Length: 52 Bit Score: 75.80 E-value: 1.03e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 847093691 14 ASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKL 65
Cdd:pfam16689 1 ASYDQLLRQVEALKLENTTLRQELRDNSSHLSKLETEASNMKEVLKHLQGSI 52
|
|
| Suppressor_APC |
pfam11414 |
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has ... |
109-182 |
1.21e-15 |
|
Adenomatous polyposis coli tumour suppressor protein; The tumour suppressor protein, APC, has a nuclear export activity as well as many different intracellular functions. The structure consists of three alpha-helices forming two separate antiparallel coiled coils.
Pssm-ID: 463275 Cd Length: 82 Bit Score: 73.83 E-value: 1.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847093691 109 LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPHAET-FSLQIDLIRQQLEFESDHLHCVLEERFGT 182
Cdd:pfam11414 7 RMKQLEQEKDVLLQGLEMVERARDWYQQQLQEVQERQKYLGANGTyFDYGSDAQQERLEFLLARIQEVNRCLGGL 81
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-415 |
3.00e-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: 59.30 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 25 DLKKENSHL--RRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPMQLEIPQKRARDE 102
Cdd:TIGR02168 665 SAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELE----------ELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 103 srtsellMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEEL---------------PHAETFSLQIDLIRQQLEF 167
Cdd:TIGR02168 735 -------LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaeaeaeieeleAQIEQLKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 168 ESDHLHcVLEERFGTADEMVQRAQIRASHLEQIEQQLEEmQSKEVKEHQVIEEKSMD----LAEKINTEAVAPPDDSSGQ 243
Cdd:TIGR02168 808 LRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEeleeLIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 244 QEskvevvfwlLSMLANRDKDDMSRTLLAMSSsqdscqamrrsgclplliqilheaerdtkapESSAFKDARMRANAALH 323
Cdd:TIGR02168 886 EE---------ALALLRSELEELSEELRELES-------------------------------KRSELRRELEELREKLA 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 324 NVifsqpDEGQAKKEMRVLHILEQIRSytetccDWMLEHERVGNMHecNPVPVEPQICQAScaIMKLsfdeeyRRAMNEL 403
Cdd:TIGR02168 926 QL-----ELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALE--NKIEDDEEEARRR--LKRL------ENKIKEL 984
|
410
....*....|....
gi 847093691 404 GG--LQAIAELLEV 415
Cdd:TIGR02168 985 GPvnLAAIEEYEEL 998
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1956-2293 |
4.61e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1956 AQAPVPSPISKRSKNTQVLPGNKTQKSPV--RIPFMKKPTPRCPPGPSPLAIEPVSP-LQSPSRRPQGSRLNQVKNsese 2032
Cdd:PHA03247 2456 ARTILGAPFSLSLLLGELFPGAPVYRRPAeaRFPFAAGAAPDPGGGGPPDPDAPPAPsRLAPAILPDEPVGEPVHP---- 2531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2033 ksgmlRQLTFIKessgSMRRQHSD-------------LSVSRQHRIPPPKNSALPAVFLCSSRCEELKVHKQP-KPKVTA 2098
Cdd:PHA03247 2532 -----RMLTWIR----GLEELASDdagdpppplppaaPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSaRPRAPV 2602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2099 SPNCPPRRTSSESPsrLPVRNLPPAPEPFKRYSSSPHINLPGPRGECRKDQNASRAEEARVSRPHTALSQDRAT------ 2172
Cdd:PHA03247 2603 DDRGDPRGPAPPSP--LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAqasspp 2680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2173 --WRR--IRD------------------EDIPHILRSTLPACALPLTDDVSEPRRKTSDAVVQTEDIAVTKTNSSTSPTL 2230
Cdd:PHA03247 2681 qrPRRraARPtvgsltsladpppppptpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847093691 2231 ESSSMGSRNRPGLASSLLPELGKSALAVVNLPTSRHSSPSRAARVTPFNYVPSPILTVTEEAA 2293
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS 2823
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1958-2277 |
4.64e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.71 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1958 APVPSPISKRSKNTQvlPGNKTQKSPVRIPFMKKPTPRCPPGPSPLAIEPVSP-LQSPSRRPQGSRLNQVKNSESEKSGM 2036
Cdd:PHA03247 2574 APRPSEPAVTSRARR--PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPdPPPPSPSPAANEPDPHPPPTVPPPER 2651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2037 LRQLTfiKESSGSMRRQHSDLSVSRQHRIPP--PKNSALPAvflcssrceelkvhkqPKPKVTASPNCPPRRTSSESPSR 2114
Cdd:PHA03247 2652 PRDDP--APGRVSRPRRARRLGRAAQASSPPqrPRRRAARP----------------TVGSLTSLADPPPPPPTPEPAPH 2713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2115 LPVRNLPPAPEPFKRYSSSPHINL-PGPRGEcrKDQNASRAEEARVSRPHTALSQDRATWRRIRDEDIPHILRSTLPACA 2193
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAaPAPPAV--PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2194 LPLTDDVSEPRRKTSDAVVQTEDIAVTKTNSSTSPTLESSSMGSRNRPGLASSLLPELGKSALAVVNLPTSRHSSPSRAA 2273
Cdd:PHA03247 2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
|
....
gi 847093691 2274 RVTP 2277
Cdd:PHA03247 2872 AAKP 2875
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
584-623 |
7.37e-07 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 47.45 E-value: 7.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 847093691 584 DDYRQILRDHNCLQTLLQHLRSHSLTIVSNACGTLWNLSA 623
Cdd:pfam00514 2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| ARM |
smart00185 |
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ... |
583-623 |
1.14e-06 |
|
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.
Pssm-ID: 214547 [Multi-domain] Cd Length: 41 Bit Score: 47.04 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 847093691 583 RDDYRQILRDHNCLQTLLQHLRSHSLTIVSNACGTLWNLSA 623
Cdd:smart00185 1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-272 |
2.88e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 6 RVGMVGAAAS--YDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFK 83
Cdd:COG4372 21 KTGILIAALSeqLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE----------ELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 84 DISATPMQLEIPQKRARDESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELpHAETFSLQIDLIRQ 163
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL-EEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 164 QLEFESDHLHCVLEErfgtADEMVQRAQIRASHLEQI-EQQLEEMQSKEVKEHQVIEEKSMDLAEKINTEAVAPPDDSSG 242
Cdd:COG4372 170 EQELQALSEAEAEQA----LDELLKEANRNAEKEEELaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270
....*....|....*....|....*....|
gi 847093691 243 QQESKVEVVFWLLSMLANRDKDDMSRTLLA 272
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEE 275
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-307 |
5.33e-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: 51.98 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 12 AAASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQvklehdvgggaghAEMLDQFKDISATPMQ 91
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ-------------KELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 92 LEIPQKRARDESRTSELLMQELEKERSLLlgEIDKEEKEKLWYYS-----QIQSLSKRLEELPHA-ETFSLQIDLIRQQL 165
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKL--DELAEELAELEEKLeelkeELESLEAELEELEAElEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 166 EFESDHLHCVLEE------RFGTADEMVQRAQIRASHLEQ-IEQQLEEMQSKEVKEHQV-IEEKSMDLAEKINTEAVAPP 237
Cdd:TIGR02168 382 ETLRSKVAQLELQiaslnnEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAeLEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 238 DDSSGQQESKvevvfwllsmLANRDKDDMSRTLLAMSSSQDSCQAMRR-------------------SGCLPLLIQILHE 298
Cdd:TIGR02168 462 ALEELREELE----------EAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkallknqsglSGILGVLSELISV 531
|
....*....
gi 847093691 299 AERDTKAPE 307
Cdd:TIGR02168 532 DEGYEAAIE 540
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-326 |
3.70e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 13 AASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhDVGGGaghaEMLDQFKDISatpmQL 92
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEE----EQLRVKEKIG----EL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 93 EIPQKRARDESRTSELLMQELEKERSLLLGEIDK--EEKEKLwyYSQIQSLSKRLEELpHAETFSLQ--IDLIRQQLEfe 168
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKllAEIEEL--EREIEEERKRRDKL-TEEYAELKeeLEDLRAELE-- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 169 sdhlhcVLEERFGTA-DEMVQRAQirasHLEQIEQQLEEMQSKEVKEHQVIEEKSMDLAEKINT-----EAVAPPDDSSG 242
Cdd:TIGR02169 375 ------EVDKEFAETrDELKDYRE----KLEKLKREINELKRELDRLQEELQRLSEELADLNAAiagieAKINELEEEKE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 243 QQESKVEVVFWLLSMLAnRDKDDMSRTLLAMSSSQDSCQAMRRSgcLPLLIQILhEAERDTKAPESSAFKDARMRANAAL 322
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSK--LQRELAEA-EAQARASEERVRGGRAVEEVLKASI 520
|
....
gi 847093691 323 HNVI 326
Cdd:TIGR02169 521 QGVH 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-233 |
8.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 12 AAASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPMQ 91
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----------EAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 92 LEIPQKRARDESRTSELLMQELEKERSLLLGEIDKEEKEKLwyySQIQSLSKRLEELPHAEtfSLQIDLIRQQLEFESDH 171
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAE--AELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 847093691 172 LHcVLEERFGTADEMVQRAQIRASHLEQIEQQLEEMQSKEVKEHQVIEEKSMDLAEKINTEA 233
Cdd:COG1196 375 AE-AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-207 |
9.52e-05 |
|
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: 47.81 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 32 HLRRELKDNSSQLNRLEHDTSDMKEvlkHLQVKLEHDVGGGAGHAEMLDQFKDISAtpmQLEIPQKRAR---DESRTSEL 108
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVSSLTA---QLESTKEMLRkvvEELTAKKM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 109 LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKR----LEELPHaetfslqidlirqqLEFESDHLHCVLEERFGTAD 184
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlkLQELQH--------------LKNEGDHLRNVQTECEALKL 555
|
170 180
....*....|....*....|...
gi 847093691 185 EMVQRAQIrashLEQIEQQLEEM 207
Cdd:pfam15921 556 QMAEKDKV----IEILRQQIENM 574
|
|
| SAMP |
pfam05924 |
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1364-1384 |
2.18e-04 |
|
SAMP Motif; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). This motif binds axin.
Pssm-ID: 461782 Cd Length: 22 Bit Score: 40.27 E-value: 2.18e-04
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-233 |
3.95e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 12 AAASYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEHDVGGGAGHAEMLDQFKD--ISATP 89
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 90 MQLEIPQKRARDESRTSELLMQELEKERSLLLGEIDKEEKEKlwyysQIQSLSKRLEELPHA-ETFSLQIDLIRQQLEFE 168
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-----AEEALLERLERLEEElEELEEALAELEEEEEEE 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847093691 169 SDHLHCVLEERFGTADEMVQRAQIRASHLEQIEQQLEEMQSKEVKEHQVIEEKSMDLAEKINTEA 233
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
17-221 |
4.76e-04 |
|
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: 45.58 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 17 DQLVRQVEDLKKENSHLRRELKDNSSQLNRL-EHDTS--------DMKevLKHLQVKLEHDVGGG---------AGHAEM 78
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELTEKESSLIDLkEHASSlassglkkDSK--LKSLEIAVEQKKEECsklenqlkkAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 79 LDQFK-DISATPMQLEIPQKRARDESRTS----ELLM---QELEKERSlllgeiDKEEK----EKLwYYSQIQSLSKRLE 146
Cdd:pfam10174 549 AVRTNpEINDRIRLLEQEVARYKEESGKAqaevERLLgilREVENEKN------DKDKKiaelESL-TLRQMKEQNKKVA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 147 ELPHAETF------SLQIDLIRQQLEFESDHLHCVLEERFGTademvqraqirashLEQIEQQLEEMQSKEVKEHQVIEE 220
Cdd:pfam10174 622 NIKHGQQEmkkkgaQLLEEARRREDNLADNSQQLQLEELMGA--------------LEKTRQELDATKARLSSTQQSLAE 687
|
.
gi 847093691 221 K 221
Cdd:pfam10174 688 K 688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-228 |
8.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 17 DQLVRQVEDLKK-ENSH-----LRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPM 90
Cdd:PRK03918 148 EKVVRQILGLDDyENAYknlgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE----------EVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 91 QLEipQKRARDESRTSEL-----LMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEEL-----------PHAETF 154
Cdd:PRK03918 218 ELR--EELEKLEKEVKELeelkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkelkEKAEEY 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 155 SLQIDLIRQQLEFESDhlhcvLEERFGTADEMVQRAQIRASHLEQIEQQLEEMQSKEVKehqvIEEKSMDLAEK 228
Cdd:PRK03918 296 IKLSEFYEEYLDELRE-----IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEER 360
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1951-2274 |
8.47e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1951 TPSRKAQAPVPSP--ISKRSKNTQVLPGNKTQKSPVRIPFMKKPTPRCPPGPS--PLAIEPVSPLQSPSrrpqgsrlnqv 2026
Cdd:PHA03307 63 DRFEPPTGPPPGPgtEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDppPPTPPPASPPPSPA----------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2027 knseSEKSGMLRqltfiKESSGSMRRQHSDLSVSRQHRIPP--PKNSALPAVFLCSSRCEElkvHKQPKPKVTASPNCPP 2104
Cdd:PHA03307 132 ----PDLSEMLR-----PVGSPGPPPAASPPAAGASPAAVAsdAASSRQAALPLSSPEETA---RAPSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2105 RRTSS-----ESPSRLPVRNLPPAPE-------PFKRYSSSPHINLP---GPRGECRKDQNASRAEEARVSRPHTALSQD 2169
Cdd:PHA03307 200 AAASPrpprrSSPISASASSPAPAPGrsaaddaGASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRIWEASGWNGPS 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2170 R-------ATWRRIRDEDIPHILRSTLPACALPLTDDVSEPRRKTSDAVVQTEDIAVTKTNSSTSPTLESSSMGSRNRPG 2242
Cdd:PHA03307 280 SrpgpassSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPP 359
|
330 340 350
....*....|....*....|....*....|..
gi 847093691 2243 LASSLLPELGKSALAVVNLPTSRHSSPSRAAR 2274
Cdd:PHA03307 360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRAR 391
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1928-2167 |
1.32e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1928 PKRSATPPARISNASSSsssrNSTPSRKAQAPVPSPISKRsknTQVLPGNKTQKSPVRIPFMKKPT-PRCPPGPSPLAIE 2006
Cdd:PHA03247 2779 PPRRLTRPAVASLSESR----ESLPSPWDPADPPAAVLAP---AAALPPAASPAGPLPPPTSAQPTaPPPPPGPPPPSLP 2851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2007 P---VSPLQSPSRRPQgSRLNQVKNSESEKSGMLRqltfikessgsmrrqhsdlsVSRQHRIPPPKNSALPAVFLCSSRC 2083
Cdd:PHA03247 2852 LggsVAPGGDVRRRPP-SRSPAAKPAAPARPPVRR--------------------LARPAVSRSTESFALPPDQPERPPQ 2910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2084 EELkvhkQPKPKVTASPNCPPRRTSSESPSRLPVRNLPPAPEPFKRYSSSPHINLP--GPRGECRKDQNASRAEEARVSR 2161
Cdd:PHA03247 2911 PQA----PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlGALVPGRVAVPRFRVPQPAPSR 2986
|
....*.
gi 847093691 2162 PHTALS 2167
Cdd:PHA03247 2987 EAPASS 2992
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
21-229 |
1.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 21 RQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQvKLEHDVgggaghAEMLDQ--------FKDISATPMQL 92
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEEL------AELLKEleelgfesVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 93 EIPQKRARdESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPHAETFSLQIDLIRQQLEFESDHL 172
Cdd:PRK03918 598 EPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 173 HcvLEERFGTADEmvQRAQIRAShLEQIEQQLEEMQSKEvKEHQVIE---EKSMDLAEKI 229
Cdd:PRK03918 677 G--LRAELEELEK--RREEIKKT-LEKLKEELEEREKAK-KELEKLEkalERVEELREKV 730
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
630-665 |
1.55e-03 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 38.20 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*.
gi 847093691 630 ELLWDLGAISMLRNLIHSKHKMIAMGSAAALRNLLA 665
Cdd:pfam00514 6 QAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
15-233 |
2.07e-03 |
|
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: 43.47 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 15 SYDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATpmqLEI 94
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK----------VLSRSINKIKQN---LEQ 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 95 PQKRArdESRTSELLM------------QELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPHAETFSL---QID 159
Cdd:TIGR04523 487 KQKEL--KSKEKELKKlneekkeleekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekEID 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 160 LIRQQLEfESDHLHCVLEERFGTADEMVQ---------RAQIRA--SHLEQIEQQLEEMQskevKEHQVIEEKSMDL--- 225
Cdd:TIGR04523 565 EKNKEIE-ELKQTQKSLKKKQEEKQELIDqkekekkdlIKEIEEkeKKISSLEKELEKAK----KENEKLSSIIKNIksk 639
|
....*...
gi 847093691 226 AEKINTEA 233
Cdd:TIGR04523 640 KNKLKQEV 647
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-221 |
2.09e-03 |
|
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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 21 RQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEH-----DVgggAGHAEMLDQFKD----ISATPMQ 91
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeiDV---ASAEREIAELEAelerLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 92 LEipqkRARDESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELPhaetfslqiDLIRQQLEFEsdh 171
Cdd:COG4913 687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE---------DLARLELRAL--- 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 847093691 172 lhcvLEERFGTADEMVQRAQIRashlEQIEQQLEEMQSKEVKEHQVIEEK 221
Cdd:COG4913 751 ----LEERFAAALGDAVERELR----ENLEERIDALRARLNRAEEELERA 792
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-235 |
2.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 12 AAASYDQLVRQVEDLKKEnsHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEHDVGggaghaemldqfkdisatpmQ 91
Cdd:COG1196 211 KAERYRELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEA--------------------E 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 92 LEipqkRARDESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEELphaetfSLQIDLIRQQLEFESDh 171
Cdd:COG1196 269 LE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL------EEELAELEEELEELEE- 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847093691 172 lhcVLEERFGTADEMVQRAQIRASHLEQIEQQLEEMQSKEVKEHQVIEEKSMDLAEKINTEAVA 235
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| APC_r |
pfam05923 |
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis ... |
1434-1456 |
3.20e-03 |
|
APC repeat; This short region is found repeated in the mid region of the adenomatous polyposis proteins (APCs). In the human protein many cancer-linked SNPs are found near the first three occurrences of the motif. These repeats bind beta-catenin.
Pssm-ID: 461781 Cd Length: 24 Bit Score: 36.97 E-value: 3.20e-03
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-229 |
3.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 34 RRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEHDVGGGAGHaEMLDQFKDI--SATPMQLEIPQKRARDESRTSELL-- 109
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELeeKLKKYNLEELEKKAEEYEKLKEKLik 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 110 --------------MQELEKERSLLLGEIDKEEKEK--------LWYYSQIQSLSKRLEEL--PHAETFSLQIdlIRQQL 165
Cdd:PRK03918 537 lkgeikslkkelekLEELKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELepFYNEYLELKD--AEKEL 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847093691 166 EFESDHLHcVLEERFGTADEMVQRAQIRashLEQIEQQLEEMQSK-EVKEHQVIEEKSMDLAEKI 229
Cdd:PRK03918 615 EREEKELK-KLEEELDKAFEELAETEKR---LEELRKELEELEKKySEEEYEELREEYLELSREL 675
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1904-2284 |
5.15e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1904 ATAVRSRSLHRLGKSSDLGVEMTLPKRSATPPARISNASSSSSSRNSTPSRKAQAPVPSPISKRSKNTQVlPGNKTQKSP 1983
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPG-PAAARQASP 2733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 1984 VripfmkKPTPRCPPGPSPLAIEPVSPlQSPSRRPQGSRLNQVKNSESEKSGMLRQLTfikessgsmRRQHSDLSVSRQH 2063
Cdd:PHA03247 2734 A------LPAAPAPPAVPAGPATPGGP-ARPARPPTTAGPPAPAPPAAPAAGPPRRLT---------RPAVASLSESRES 2797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2064 RIPPPKNSALPAVFLCSSRCEelkvhkqPKPKVTASPNCPPRRTSSESPsrlpvrnlPPAPEPFKRYSSSPHINLPGPRG 2143
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAAL-------PPAASPAGPLPPPTSAQPTAP--------PPPPGPPPPSLPLGGSVAPGGDV 2862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 2144 ECRKDQNASRAEEARVSRPhtalsqdratwrRIRDEDIPHILRSTLPacaLPLTDDvSEPRRKTSDAVVQTEDIAVTKTN 2223
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARP------------PVRRLARPAVSRSTES---FALPPD-QPERPPQPQAPPPPQPQPQPPPP 2926
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 847093691 2224 SSTSPTLESSsmgSRNRPGLASSLLPELGKSALAVVNLPTSRHSSPSRAArvTPFNYVPSP 2284
Cdd:PHA03247 2927 PQPQPPPPPP---PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA--VPRFRVPQP 2982
|
|
| EB1_binding |
pfam05937 |
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the ... |
2263-2284 |
5.28e-03 |
|
EB-1 Binding Domain; This region, found at the C-terminus of the APC proteins, binds the microtubule-associating protein EB-1. At the C-terminus of the alignment is also a pfam00595 binding domain. A short motif in the middle of the region appears to be found in the APC2 proteins.
Pssm-ID: 399141 Cd Length: 174 Bit Score: 39.98 E-value: 5.28e-03
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
17-220 |
6.91e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 17 DQLVRQVEDLKKENSHLRRELKDNSSQLNRLehdtsdmKEVLKHLQVKLEHdvgggaGHAEMLDQFKDIsatpMQLEipQ 96
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKRL-------TEPLQKAQEEVEE------LRKQLENYEKDK----QSLK--N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 97 KRARDESRTSELlmQELEKERSLLLGEIDKEEKEKlwyysqiQSLSKRLEELPHaETF---SLQIDLIRQQLEfesdHLH 173
Cdd:pfam13851 90 LKARLKVLEKEL--KDLKWEHEVLEQRFEKVERER-------DELYDKFEAAIQ-DVQqktGLKNLLLEKKLQ----ALG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 847093691 174 CVLEERFGTADEMVQRAQIRASHLEQIEQQLEE-MQSKevkeHQVIEE 220
Cdd:pfam13851 156 ETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDvLESK----NQLIKD 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-210 |
7.90e-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: 41.58 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 16 YDQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEHdvgggaghaemldqfkdisatpmqleip 95
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA---------------------------- 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 96 qkrARDESRTSELLMQELEKERSLLLGEIDKEEKEKLWYYSQIQSLSKRLEelphaetfslQIDLIRQQLEFESDHLHCV 175
Cdd:TIGR02168 878 ---LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA----------QLELRLEGLEVRIDNLQER 944
|
170 180 190
....*....|....*....|....*....|....*.
gi 847093691 176 LEERFG-TADEMVQRAQIRASHLEQIEQQLEEMQSK 210
Cdd:TIGR02168 945 LSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-234 |
8.51e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 17 DQLVRQVEDLKKENSHLRRELKDNSSQLNRLEHDTSDMKEVLKHLQVKLEhdvgggaghaEMLDQFKDISATPMQLEIPQ 96
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI----------DLKEQIKSIEKEIENLNGKK 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847093691 97 KRARDESRTSELLMQELEKERSLLLGEIDKEEKeklwyysQIQSLSKRLEELphaetfSLQIDLIRQQLEfesdhlhcVL 176
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEA-------QLRELERKIEEL------EAQIEKKRKRLS--------EL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 847093691 177 EERFGTADEmvQRAQIRASHLEQIEQQLEEMQSKEVKEH-QVIEEKSMDLaEKINTEAV 234
Cdd:TIGR02169 923 KAKLEALEE--ELSEIEDPKGEDEEIPEEELSLEDVQAElQRVEEEIRAL-EPVNMLAI 978
|
|
| |
