|
Name |
Accession |
Description |
Interval |
E-value |
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
4063-4138 |
3.83e-37 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 135.65 E-value: 3.83e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 4063 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 4138
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
4065-4139 |
3.43e-35 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 129.64 E-value: 3.43e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 4065 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 4139
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3163-3379 |
2.12e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 118.70 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3163 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 3242
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3243 RLETMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 3322
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 3323 REETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHAVSSKMEERKSKLEEAL 3379
Cdd:cd00176 158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3603-3815 |
9.52e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 116.78 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 3762
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 3763 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 3815
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3384-3598 |
1.19e-27 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 113.69 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3384 EFQNSLQEFINWLTLAEQSLNIASPPSlILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 3463
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3464 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 3543
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 3544 PVYDTTIRTGRALKEKtLLPEDTQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 3598
Cdd:cd00176 160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2943-3160 |
1.39e-23 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 101.75 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2943 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 3022
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3023 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 3102
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833258 3103 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 3160
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2177-2390 |
1.80e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 95.98 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 2336
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 2337 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLEQAL 2390
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3055-3269 |
9.27e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 93.66 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3055 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 3134
Cdd:cd00176 4 QFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3135 LTELKHLWENLGEKIAHRQHKLEGALLALgQFQHALEELMSWLTHTEELLDAQrPISGDPKVIEVELAKHHVLKNDVLAH 3214
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 3215 QATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTL 3269
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2722-2941 |
1.43e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 87.50 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2722 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 2801
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2802 KAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSrlrmpPLIPAEVDKIRECISDNKSATVELEK 2881
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2882 LQPSFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 2941
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1522-1736 |
2.11e-16 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 80.95 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1522 YQELLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 1601
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1602 ETVALPLQGLEDLAADRMNRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHS 1681
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 1682 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 1736
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3165-3266 |
6.21e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 73.13 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3165 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 3244
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 3245 ETMNQCWESVLQKTEEREQQLQ 3266
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2612-2824 |
5.10e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.32 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2612 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 2691
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2692 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEH 2771
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 2772 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYHKAENMYAQIKEEVRQRALALDEA 2824
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
712-940 |
6.35e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.94 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 712 ELQKFLQDHREFESWLERSEKELENMHkGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDtensfkEGKEP 791
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 792 SEIgnlVKDKLKDATERYTALHSECTRLGFHLNMLLgQYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLA 871
Cdd:cd00176 74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEA---ALASEDLGKDLESVEELLK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 872 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAI 940
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
928-1694 |
7.97e-13 |
|
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: 75.48 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 928 SLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 1007
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1008 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrff 1087
Cdd:TIGR02168 324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL--------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1088 qQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 1167
Cdd:TIGR02168 394 -QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1168 FQKWLKETEGSIpptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapDSQGKTGSILPSVGS 1247
Cdd:TIGR02168 473 AEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALL----------------KNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1248 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGilherqeSLQAILNRMEEVQKEANSVLQWLESKEE---VLKSMDAMS 1324
Cdd:TIGR02168 528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1325 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIEEE-----------LNSRW------ 1387
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1388 ERATEVTVARQRQLEESAGHLASFQAAESQLRPW--MMEKEL--MMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 1463
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAlaELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1464 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQR 1539
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1540 LSG----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSVLIgeqylkDELKKRLETVALPLQGLEDLA 1615
Cdd:TIGR02168 826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESEL------EALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 1616 ADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESL 1694
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-----LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3603-3703 |
9.33e-13 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.97 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLE 3703
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1762-2641 |
1.58e-12 |
|
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: 74.32 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1762 ELRVTLDPVQLESSLLRskaMLSEVEKRRSLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAITEELQAK 1835
Cdd:TIGR02168 217 ELKAELRELELALLVLR---LEELREELEELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAP 1915
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1916 DGSDASQLLHQAEVTQQEFLEvkqRVNSGCVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAVGRDtdsLQSQIED 1995
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1996 VRLFLNKIQVVKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLn 2075
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2076 dattaAEEAEALQWVVGTEVEIINqqladfkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW 2154
Cdd:TIGR02168 512 -----LKNQSGLSGILGVLSELIS-------------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2155 ----------NTLNKKVAQRIAQLQEALLHCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiq 2214
Cdd:TIGR02168 574 tflpldsikgTEIQGNDREILKNIEGFLGVAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT---- 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2215 eqkllqrlLDDRKATVDML------QAEGGRIAQSAELADREKitgQLKSLESRWTELLSKAAARQKQLEDILVLAKQFH 2288
Cdd:TIGR02168 650 --------LDGDLVRPGGVitggsaKTNSSILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2289 ETAEPISDFLSVTEKKLANSE-PVGTQTAKIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDS 2367
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEaEVEQLEERIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2368 LQARYSEIQDRCcrkaALLEQALSNARlfgedevevlnwlAEVEDKLSSVFVKDFKQDVLHKQHADHLALNEEIVNRKKN 2447
Cdd:TIGR02168 787 LEAQIEQLKEEL----KALREALDELR-------------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2448 V-DQAIKNGQALLKQTTGEEVLliQEKLDGIktrytditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAAs 2526
Cdd:TIGR02168 850 LsEDIESLAAEIEELEELIEEL--ESELEAL-----------LNERASLEEALALL---RSELEELSEELRELESKRSE- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2527 ggqsptgeqipqFQQRQKELKKEVMEHRLVLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDA 2606
Cdd:TIGR02168 913 ------------LRRELEELREKLAQLELRLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
890 900 910
....*....|....*....|....*....|....*
gi 1622833258 2607 AIQRSQQYeqaadaelawVAETKRKLMALGPIRLE 2641
Cdd:TIGR02168 966 DEEEARRR----------LKRLENKIKELGPVNLA 990
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1297-1516 |
3.15e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.01 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1297 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 1376
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1377 KKIEEELNSRWERATEVTVARQRQLEESAGhLASFQAAESQLRPWMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 1456
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1457 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAI 1516
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3493-3595 |
7.27e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 64.66 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3493 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDTQKLDNF 3572
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833258 3573 LGEVRDKWDTVCGKSVERQHKLE 3595
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3165-3266 |
1.21e-11 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 63.88 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3165 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 3244
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
|
90 100
....*....|....*....|..
gi 1622833258 3245 ETMNQCWESVLQKTEEREQQLQ 3266
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLE 104
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
3988-4050 |
1.24e-10 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 59.87 E-value: 1.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 3988 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 4050
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
3988-4058 |
1.49e-10 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 62.12 E-value: 1.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622833258 3988 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 4058
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2393-2608 |
9.26e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 61.69 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2393 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 2472
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2473 KLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELaASGGQSPTGEQIPQFQQRQKELKKEVME 2552
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 2553 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 2608
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1381-2101 |
1.26e-09 |
|
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: 65.08 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1381 EELNSRWERATEVTVARQRQLEESAGHLASFQAAESQLRPWM----MEKELMMGVLGPLSIDPNMLNAQKQ-------QV 1449
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleEEIEELQKELYALANEISRLEQQKQilrerlaNL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1450 QFMLKEFEARRQQHEQLNEAAQGILTgpgdvslstsQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDL 1529
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1530 SEKVRAVGQRLSGQSAistqpeavkqqleETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKdELKKRLETVAlplQ 1609
Cdd:TIGR02168 385 RSKVAQLELQIASLNN-------------EIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---E 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1610 GLEDLAAdRMNRLQAALASTqqfQQMFDELRTWLDDKQSQQAKncpISAKLERLHSQLQENEEFQKS-----LNQHSGSY 1684
Cdd:TIGR02168 448 ELEELQE-ELERLEEALEEL---REELEEAEQALDAAERELAQ---LQARLDSLERLQENLEGFSEGvkallKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1685 EVIVAegeSLLLSVPPGEEK-------RTLQNQLVELKNHWEE----LSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWI 1753
Cdd:TIGR02168 521 ILGVL---SELISVDEGYEAaieaalgGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1754 EDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSAADI------LINSSEADEDGIRDEKAGI---NQ 1823
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRkALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPGGVITGGSAKTNSSIlerRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1824 NMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQAcsNKNLEKLRAQQE-VLQALEPQVDY 1902
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEqLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1903 LRNFTQGLVEDAPDGSDASQLLHQAEVTQQeflEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQL-ADLDDELDGMGA 1981
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQIEQ----LKEELKALREALDELRAELTLLnEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1982 VGRDTDSLQSQIEDVRlflNKIQVVKLDIEASEAECRHM--LEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLEL 2059
Cdd:TIGR02168 829 LERRIAATERRLEDLE---EQIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1622833258 2060 TLGRVEDFYRKLKGLNDATTAAEEAEAlqwvvGTEVEIINQQ 2101
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLE-----GLEVRIDNLQ 942
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2177-2278 |
2.93e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLE 2278
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3055-3157 |
3.22e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3055 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 3134
Cdd:smart00150 2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833258 3135 LTELKHLWENLGEKIAHRQHKLE 3157
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2722-2822 |
6.25e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.18 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2722 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 2801
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 2802 KAENMYAQIKEEVRQRALALD 2822
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1630-1733 |
6.50e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.18 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1630 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 1709
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833258 1710 QLVELKNHWEELSKKTADRQSRLK 1733
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
3986-4049 |
1.54e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.80 E-value: 1.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 3986 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 4049
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
320-556 |
7.49e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 55.91 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 320 QLEGRLQDLRAWVGNTILILNSkgSNSETDVDSLNRCLQQYEDLKQPMAERKSQLDALAFDVQFFISEHAQDLSPQQNRq 399
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 400 mlrlLNELQRSFQEILEQTAAQVDALQGHLQQMEQealvktlqkqqntcHQQLEDLCSWVGQAERALAGHQgrtTRQDLS 479
Cdd:cd00176 81 ----LEELNQRWEELRELAEERRQRLEEALDLQQF--------------FRDADDLEQWLEEKEAALASED---LGKDLE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 480 ALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsPHELTALREKLHQAKEQYEALREQTRVAQKELEEA 556
Cdd:cd00176 140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1630-1734 |
9.98e-08 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 52.71 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1630 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 1709
Cdd:pfam00435 4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
|
90 100
....*....|....*....|....*
gi 1622833258 1710 QLVELKNHWEELSKKTADRQSRLKD 1734
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3603-3704 |
1.79e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 52.32 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLEQ 3704
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1294-1403 |
1.97e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.94 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1294 NRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 1373
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
|
90 100 110
....*....|....*....|....*....|
gi 1622833258 1374 ENWKKIeEELNSRWERATEVTVARQRQLEE 1403
Cdd:pfam00435 77 EIQERL-EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
829-937 |
3.64e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.17 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 829 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 908
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
|
90 100
....*....|....*....|....*....
gi 1622833258 909 KHVQETTDSILSHFQSLSYSLAERSSLLQ 937
Cdd:pfam00435 76 EEIQERLEELNERWEQLLELAAERKQKLE 104
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2177-2279 |
1.71e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 49.24 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLED 2279
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-713 |
1.83e-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: 54.68 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTA-AQVDALQGHLQQMEQEALVKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRT 473
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-----SKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 474 TRQDL----SALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEEnqtklspheLTALREKLHQAKEQYEALREQTRVA 549
Cdd:TIGR02168 766 LEERLeeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE---------LTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 550 QKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLltnlpgMEQLSKASLEKGTLDTTDgymgvnq 629
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEELSEEL------- 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 630 apEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTL 709
Cdd:TIGR02168 904 --RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
....
gi 1622833258 710 QDEL 713
Cdd:TIGR02168 981 IKEL 984
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3380-3486 |
3.19e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 48.47 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3380 NLATEFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLI 3459
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833258 3460 KNLLVSVQSRWEKVVQRSIERGRSLDD 3486
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1297-1402 |
4.89e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1297 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 1376
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833258 1377 KKIEEELNSRWERATEVTVARQRQLE 1402
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-735 |
5.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 385 ISEHAQDLSPQQNRQMLRLLNELQRSFQEI--LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQA 462
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELkeAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 463 ERALAGHQGRTTRQDLS----ALQKNQSDLKDLQDDIQNHATSFAAVVKDIEgfMEENQTKLspheltALREKLHQAKEQ 538
Cdd:COG4717 129 PLYQELEALEAELAELPerleELEERLEELRELEEELEELEAELAELQEELE--ELLEQLSL------ATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 539 YEALREQTRVAQKELEEAVT--SALQQETEKSKAAKELAENKKKIDALLDWVTSVgssGGQLLTNLPGMEQLSKASLEKG 616
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEelEELEEELEQLENELEAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 617 TLDTTDGYMGVnqAPEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHG--HNLTPEEQQMLQEKLGELKEQYSt 694
Cdd:COG4717 278 VLFLVLGLLAL--LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLR- 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622833258 695 SLAQSEAELkQVQTLQDELQKFLQ-----DHREFESWLERSEKELE 735
Cdd:COG4717 355 EAEELEEEL-QLEELEQEIAALLAeagveDEEELRAALEQAEEYQE 399
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2205-2768 |
5.73e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2205 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLKSLESRWTELLSKAAARQKQLEDIL-VL 2283
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2284 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 2357
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2358 QGVLSEKIDSLQARYSEIQDRCCRKAALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHADHLAL 2437
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2438 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYTDIT---------VTSSKALRTLEQARQLATKFQst 2508
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2509 yeELTGWLREVE---EELAASGGQSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 2580
Cdd:COG1196 528 --VLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2581 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 2660
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2661 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 2740
Cdd:COG1196 685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1622833258 2741 IAQLPPPAIDHEQLRQQQEEMRQLRESI 2768
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
395-586 |
6.03e-06 |
|
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: 52.07 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQ-----EALVKTLQKQQNTCHQQLEDLCSWVGQAERALAgh 469
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaalEAELAELEKEIAELRAELEAQKEELAELLRALY-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 470 qgRTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsphELTALREKLHQAKEQYEALREQTRVA 549
Cdd:COG4942 115 --RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA------ELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622833258 550 QKELEEA-------VTSALQQETEKSKAAKELAENKKKIDALLD 586
Cdd:COG4942 187 RAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3825-3949 |
8.85e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3825 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 3903
Cdd:smart00150 7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622833258 3904 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 3949
Cdd:smart00150 78 ----------------------RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
831-937 |
4.08e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 831 HQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDHKH 910
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQ---LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE---EGHPDAEE 74
|
90 100
....*....|....*....|....*..
gi 1622833258 911 VQETTDSILSHFQSLSYSLAERSSLLQ 937
Cdd:smart00150 75 IEERLEELNERWEELKELAEERRQKLE 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2713-2946 |
4.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2713 LERAQVLVNQFWETYEELSPWIEETRALIAQLPPPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 2792
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2793 GEMVEEKYHKAENMyaqikEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipAEVDKIRECISDN 2872
Cdd:PRK03918 265 EERIEELKKEIEEL-----EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------EEINGIEERIKEL 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 2873 KSATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 2946
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2942-3048 |
1.10e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 44.23 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2942 ELAEKFWYDMAALLTTIKDTQDIVHDlESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFAcGETEKPEV 3021
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833258 3022 RKSIDEMNNAWENLNKTWKERLEKLED 3048
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1484-1861 |
1.35e-04 |
|
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: 48.09 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1484 TSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSGQSA----ISTQPEAVKQQLEE 1559
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1560 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRMNRLQAALASTQQFQQMFD 1637
Cdd:TIGR04523 307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1638 ELRTWLDDKQSQQAKNCPISAKLERLHSQLQE----NEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 1712
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1713 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSE 1785
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 1786 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVE 1861
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2728-2823 |
1.64e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.85 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2728 EELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYHKAENMY 2807
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
|
90
....*....|....*.
gi 1622833258 2808 AQIKEEVRQRALALDE 2823
Cdd:pfam00435 90 EQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1737-1841 |
2.15e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.46 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1737 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRD 1816
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1622833258 1817 EKAGINQNMDAITEELQAKTGSLEE 1841
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
358-584 |
2.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 358 QQYEDLKQPMAERKSQLDALAFDVQ----------FFISEHAQ---DLSPQQNRQMLRL-LNELQRSFQEILEQT---AA 420
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQklqrlhqafsRFIGSHLAvafEADPEAELRQLNRrRVELERALADHESQEqqqRS 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 421 QVDALQGHLQQMEQEA------LVKTLQKQQNTCHQQLEDLcswvGQAERALAGHQGRTTR--QDLSALQKNQSDLKDLQ 492
Cdd:PRK04863 866 QLEQAKEGLSALNRLLprlnllADETLADRVEEIREQLDEA----EEAKRFVQQHGNALAQlePIVSVLQSDPEQFEQLK 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 493 DD----------IQNHATSFAAVVK--------DIEGFMEENQtKLSPheltALREKLHQAKEQYEALREQTRVAQKELE 554
Cdd:PRK04863 942 QDyqqaqqtqrdAKQQAFALTEVVQrrahfsyeDAAEMLAKNS-DLNE----KLRQRLEQAEQERTRAREQLRQAQAQLA 1016
|
250 260 270
....*....|....*....|....*....|..
gi 1622833258 555 EA--VTSALQqeTEKSKAAKELAENKKKIDAL 584
Cdd:PRK04863 1017 QYnqVLASLK--SSYDAKRQMLQELKQELQDL 1046
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1440-1997 |
3.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1440 NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTgpgdvslSTSQVQKELQSINQKWVELTDKL----NSRSTQIDQA 1515
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLE-------EHEERREELETLEAEIEDLRETIaeteREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1516 IVKSTQYQELLQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEETSE------------------IRSDLEQLDHEVKEA 1577
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleecrvaaqahneeaesLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1578 QTLCDELSVLIgeQYLKDELKKRLETVAlplqGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpIS 1657
Cdd:PRK02224 362 REEAAELESEL--EEAREAVEDRREEIE----ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE---LE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1658 AKLERLHSQLQENEEFQKSLNQHSGSYEVivaEGESLLLSVPPGEEKR-TLQNQLVELKNHWEELSKKTaDRQSRLKDCM 1736
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPV---EGSPHVETIEEDRERVeELEAELEDLEEEVEEVEERL-ERAEDLVEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1737 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAmlseVEKRrslleilNSAADILINSSEAdedgiRD 1816
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA----EEKR-------EAAAEAEEEAEEA-----RE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1817 EKAGINQNMDAITEELQaktgSLEemtqRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQacsnkNLEKLRAQQEVLQAL 1896
Cdd:PRK02224 573 EVAELNSKLAELKERIE----SLE----RIRTLLAAIADAEDEIERLREKREALAELNDE-----RRERLAEKRERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1897 EPQVDYLRnftqglVEDA-PDGSDASQLLHQAEVTQQEFLEVKQRVNSGCVMMENKLEgigqfhcRVREMFSQLADLDDE 1975
Cdd:PRK02224 640 EAEFDEAR------IEEArEDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------ELEELRERREALENR 706
|
570 580
....*....|....*....|..
gi 1622833258 1976 LDGMGAVGRDTDSLQSQIEDVR 1997
Cdd:PRK02224 707 VEALEALYDEAEELESMYGDLR 728
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2686-2946 |
6.47e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2686 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpppaidhEQLR 2755
Cdd:COG0497 116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2756 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYHKAENmYAQIKEEVRQRALALDE------ 2823
Cdd:COG0497 179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2824 -----AVSQSAQITEFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 2888
Cdd:COG0497 244 dllgqALRALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833258 2889 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 2946
Cdd:COG0497 311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
479-777 |
7.13e-04 |
|
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: 45.53 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 479 SALQKNQSDLKDLQDDIQNHATSFAAvvkdiegfmEENQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAvt 558
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 559 salqqETEKSKAAKELAENKKKIDALLDWVtsvgssggQLLTNLPGMEQLSKASlekGTLDTTDGYMGVNQAPEKLDKHC 638
Cdd:COG4942 89 -----EKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 639 EKMKARHQELLSQQQHFILATQSAQAFLDqhghnltpeEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQ 718
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLA---------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 719 DHREFESWLERSEKELENMHKGGSSPEA-----LP---SLLKRQGSFSEDVISHKGdlrfVTISGQK 777
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALkgklpWPvsgRVVRRFGERDGGGGRNKG----IDIAAPP 286
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
234-733 |
1.27e-03 |
|
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: 45.10 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 234 LLCQAKVLDRELKDLTTLVSQELECVNQiiISQPQEVPAQLLKALEKDAKNLQKSLSSVSDTWNsRLLYFQNAVEIE--- 310
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQ--LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-RSMSTQKALEEDlqi 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 311 KTKVLNQHT-QLEGRLQDL-RAWVGNTILIlnskgSNSETDVDSLNRCLQQYEdlkQPMAERKSQLDALAFDVQFFISEH 388
Cdd:pfam05483 322 ATKTICQLTeEKEAQMEELnKAKAAHSFVV-----TEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 389 AQDLSPQQNRQM-LRLLNELQRSFQEILEQTaAQVDALQGHLQQMEQEaLVKTLQKQQNTCH-----------------Q 450
Cdd:pfam05483 394 EEMTKFKNNKEVeLEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQE-LIFLLQAREKEIHdleiqltaiktseehylK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 451 QLEDLCSWVGQAE---RALAGHQGRTTRQDLSALQKNQS---DLKDLQDDIQNHATSFAAVVKDIEGfMEENQTKLSpHE 524
Cdd:pfam05483 472 EVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLR-DE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 525 LTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQET---EKSKAAKELAENKKK-IDALLDWVTSVGSSGGQLLT 600
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKileNKCNNLKKQIENKNKnIEELHQENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 601 NLPGME------QLSKASLEKGTLDTTDGYMGVNQ----APEKLDKHCEKMKARHQELLSQQQHFILATQ----SAQAFL 666
Cdd:pfam05483 630 QLNAYEikvnklELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaEMVALM 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 667 DQHGHnltpEEQQMLQEKLGEL-----KEQYSTSLAQS-EAELKQVQTLQDELQKFLQDHREFESWLERSEKE 733
Cdd:pfam05483 710 EKHKH----QYDKIIEERDSELglyknKEQEQSSAKAAlEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
449-554 |
1.91e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 449 HQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENqtklsPHELTAL 528
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833258 529 REKLHQAKEQYEALREQTRVAQKELE 554
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1388-1895 |
2.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1388 ERATEVTVARQRQLEESAGHLASFQAAESQLRPwmMEKELmmgvlgplsidpnmlnAQKQQVQFMLKEFEAR-------- 1459
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LEQRL----------------RQQQRAERLLAEFCKRlgknldde 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1460 ------RQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQ-------SINQKWVELTDKLNSRSTQIDQAIVKSTQYQELL 1526
Cdd:PRK04863 554 deleqlQEELEARLESLSESVSEARERRMALRQQLEQLQariqrlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYM 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1527 QDLSEKVRAVGQRLSGqsaISTQPEAVKQQLEETSEIR-SDLEQLdhevkeaQTLCDELS-VLIGEQY----LKDE---- 1596
Cdd:PRK04863 634 QQLLERERELTVERDE---LAARKQALDEEIERLSQPGgSEDPRL-------NALAERFGgVLLSEIYddvsLEDApyfs 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1597 ----------LKKRLETVALPLQGLEDLAAD-----------RMNRLQAAL---ASTQQF-------------------- 1632
Cdd:PRK04863 704 alygparhaiVVPDLSDAAEQLAGLEDCPEDlyliegdpdsfDDSVFSVEElekAVVVKIadrqwrysrfpevplfgraa 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1633 -QQMFDELRTWLDDKQSQQAKNCPISAKLERLHsqlqenEEFQKSLNQHSgsyevivaegeSLLLSVPPGEEKRTLQNQL 1711
Cdd:PRK04863 784 rEKRIEQLRAEREELAERYATLSFDVQKLQRLH------QAFSRFIGSHL-----------AVAFEADPEAELRQLNRRR 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1712 VELKNHWEELSKKTADRQSRLKDCMQKAQKYQWH--------VEDLVPWIEDCKAKMSELRVT-------------LDPV 1770
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQLDEAEEAkrfvqqhgnalaqLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1771 ------------QLESSLLRSKAMLSEVEKRRSLLEILNS---------AADILINSSEADEDgIRDEKAGINQNMDAIT 1829
Cdd:PRK04863 927 vsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSDLNEK-LRQRLEQAEQERTRAR 1005
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 1830 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLeifDALGSQACSNKnLEKLRAQQEVLQA 1895
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADSGA-EERARARRDELHA 1067
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
4221-4395 |
2.78e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4221 PSSPATPASGTKTSLQFSRcYDKPWLVNSKAGTPIRDSHSPDLQLPSPEVISSS--------GSKLKRPTPTFHSSRTSL 4292
Cdd:PHA03307 84 SRSTPTWSLSTLAPASPAR-EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEmlrpvgspGPPPAASPPAAGASPAAV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4293 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLLETQSAcSDT 4356
Cdd:PHA03307 163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGASSSD-SSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622833258 4357 SES--SAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 4395
Cdd:PHA03307 242 SESsgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1740-1840 |
2.90e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1740 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 1819
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 1820 GINQNMDAITEELQAKTGSLE 1840
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1373-1940 |
3.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1373 AENWKKIEEELN--------SRWERATEVTVARQRQLEESAGHLASFQAAESQLrpwmmEKElmmgvlgplsidpnmLNA 1444
Cdd:COG1196 212 AERYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEAELAEL-----EAE---------------LEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1445 QKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQE 1524
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1525 LLQDLSEKV--------RAVGQRLSGQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDE 1596
Cdd:COG1196 352 ELEEAEAELaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1597 LKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKS 1676
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1677 LNQHSGSYEVIVAEGESLLLSVPPGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQ 1740
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1741 KYQWHVEDLVpwiedckakMSELRVTLDPVQLESSLLRSKAMLSEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAG 1820
Cdd:COG1196 587 ALAAALARGA---------IGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1821 INQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQV 1900
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622833258 1901 DYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQR 1940
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1523-2059 |
5.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1523 QELLQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEET----SEIRSDLEQLDHEVKEAQTLCDELSVLIGEQylkDELK 1598
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELEELKEEI---EELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1599 KRLETVALPLQGLEdlaaDRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKSLN 1678
Cdd:PRK03918 245 KELESLEGSKRKLE----EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1679 QHSGSYEVIVAEGESLllsvppGEEKRTLQNQLVELKNHWEELsKKTADRQSRLKDCMQKAQKYQWHVEDLVPwiEDCKA 1758
Cdd:PRK03918 321 EEINGIEERIKELEEK------EERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTP--EKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1759 KMSELRVTLDPVQLESSLLRSK--AMLSEVEKRRSLLEILNSAADIL-INSSEADEdgirDEKAGInqnMDAITEELQAK 1835
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGKCpVCGRELTE----EHRKEL---LEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQRLKEFQESFKNIEKKVEGAKH---QLEIFDALGS--QACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGL 1910
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESElikLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1911 VEDApdgSDASQLLHQAEVTQQEFLEVKQRVNSgcvmMENKLEGIGqfhcrvremFSQLADLDDELDGMGAVGRDTDSLQ 1990
Cdd:PRK03918 545 KKEL---EKLEELKKKLAELEKKLDELEEELAE----LLKELEELG---------FESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 1991 SQIEDVRLFLNKIQVVKLDIEASEAEcrhmLEEEGTlDLLGLKRELEALNKQCGKLTERGKaRQEQLEL 2059
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEE----LAETEK-RLEELRKELEELEKKYSEEEYEEL-REEYLEL 671
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
4063-4138 |
3.83e-37 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 135.65 E-value: 3.83e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 4063 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 4138
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
4065-4139 |
3.43e-35 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 129.64 E-value: 3.43e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 4065 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 4139
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3163-3379 |
2.12e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 118.70 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3163 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 3242
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3243 RLETMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 3322
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 3323 REETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHAVSSKMEERKSKLEEAL 3379
Cdd:cd00176 158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3603-3815 |
9.52e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 116.78 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 3762
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 3763 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 3815
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3384-3598 |
1.19e-27 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 113.69 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3384 EFQNSLQEFINWLTLAEQSLNIASPPSlILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 3463
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3464 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 3543
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 3544 PVYDTTIRTGRALKEKtLLPEDTQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 3598
Cdd:cd00176 160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3490-3706 |
1.73e-25 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 107.53 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3490 RAKQFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDTQKL 3569
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3570 DNFLGEVRDKWDTVCGKSVERQHKLEEALLFSgQFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKEL 3649
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833258 3650 GKRTGTVQVLKRSGRELIENSR-DDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQAL 3706
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2943-3160 |
1.39e-23 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 101.75 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2943 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 3022
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3023 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 3102
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833258 3103 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 3160
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2177-2390 |
1.80e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 95.98 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 2336
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 2337 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLEQAL 2390
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3055-3269 |
9.27e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 93.66 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3055 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 3134
Cdd:cd00176 4 QFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3135 LTELKHLWENLGEKIAHRQHKLEGALLALgQFQHALEELMSWLTHTEELLDAQrPISGDPKVIEVELAKHHVLKNDVLAH 3214
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 3215 QATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTL 3269
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2722-2941 |
1.43e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 87.50 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2722 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 2801
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2802 KAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSrlrmpPLIPAEVDKIRECISDNKSATVELEK 2881
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2882 LQPSFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 2941
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3708-3952 |
1.55e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 87.50 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3708 QAEVFRDTVHMLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIK 3787
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3788 HWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELlawiQWAETTLIQRDQEPIPQNIDRVKALIAEHQTFMEE 3867
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE----QWLEEKEAALASEDLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3868 MTRKQPDVDRVTKtykrkniepTHAPFIEKSRSGGRkslsqptpppmpilsqsEAKNPRINQLSARWQQVWLLALERQRK 3947
Cdd:cd00176 155 LEAHEPRLKSLNE---------LAEELLEEGHPDAD-----------------EEIEEKLEELNERWEELLELAEERQKK 208
|
....*
gi 1622833258 3948 LNDAL 3952
Cdd:cd00176 209 LEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3271-3488 |
2.97e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 86.35 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3271 QAQGFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKAREETYNQLLDKGRLMLlsRDDSGSGSKT 3350
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI--EEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3351 EQSVALLEQKWHAVSSKMEERKSKLEEALNLATEFQnSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANEV 3430
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833258 3431 NAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDAR 3488
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2088-2281 |
1.57e-16 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 81.34 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2088 QWVVGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQ 2167
Cdd:cd00176 25 STDYGDDLESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE--IQERLEELNQRWEELRELAEERRQR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2168 LQEALLHCGKFQDALEpLLSWLADTEELIANQKPPSAEYKvVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA 2247
Cdd:cd00176 102 LEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD 179
|
170 180 190
....*....|....*....|....*....|....
gi 1622833258 2248 DREKITGQLKSLESRWTELLSKAAARQKQLEDIL 2281
Cdd:cd00176 180 ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1522-1736 |
2.11e-16 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 80.95 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1522 YQELLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 1601
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1602 ETVALPLQGLEDLAADRMNRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHS 1681
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 1682 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 1736
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2283-2499 |
4.37e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.10 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2283 LAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAkIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLS 2362
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2363 EKIDSLQARYSEIQDRCCRKAALLEQALSNARLFgEDEVEVLNWLAEVEDKLSSVFVKDFKQDVlHKQHADHLALNEEIV 2442
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 2443 NRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYTDITVTSSKALRTLEQAR 2499
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3165-3266 |
6.21e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 73.13 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3165 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 3244
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 3245 ETMNQCWESVLQKTEEREQQLQ 3266
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1630-1842 |
2.02e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.17 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1630 QQFQQMFDELRTWLDDKQSQQAKNCPISaKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 1709
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1710 QLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQwHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKR 1789
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 1790 RSLLEILNSAADILINSSEADEDGIRDEKA-GINQNMDAITEELQAKTGSLEEM 1842
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLeELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2612-2824 |
5.10e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.32 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2612 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 2691
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2692 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEH 2771
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 2772 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYHKAENMYAQIKEEVRQRALALDEA 2824
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
712-940 |
6.35e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.94 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 712 ELQKFLQDHREFESWLERSEKELENMHkGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDtensfkEGKEP 791
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 792 SEIgnlVKDKLKDATERYTALHSECTRLGFHLNMLLgQYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLA 871
Cdd:cd00176 74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEA---ALASEDLGKDLESVEELLK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 872 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAI 940
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
928-1694 |
7.97e-13 |
|
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: 75.48 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 928 SLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 1007
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1008 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrff 1087
Cdd:TIGR02168 324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL--------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1088 qQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 1167
Cdd:TIGR02168 394 -QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1168 FQKWLKETEGSIpptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapDSQGKTGSILPSVGS 1247
Cdd:TIGR02168 473 AEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALL----------------KNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1248 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGilherqeSLQAILNRMEEVQKEANSVLQWLESKEE---VLKSMDAMS 1324
Cdd:TIGR02168 528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1325 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIEEE-----------LNSRW------ 1387
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1388 ERATEVTVARQRQLEESAGHLASFQAAESQLRPW--MMEKEL--MMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 1463
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAlaELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1464 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQR 1539
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1540 LSG----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSVLIgeqylkDELKKRLETVALPLQGLEDLA 1615
Cdd:TIGR02168 826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESEL------EALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 1616 ADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESL 1694
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-----LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3603-3703 |
9.33e-13 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.97 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLE 3703
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1762-2641 |
1.58e-12 |
|
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: 74.32 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1762 ELRVTLDPVQLESSLLRskaMLSEVEKRRSLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAITEELQAK 1835
Cdd:TIGR02168 217 ELKAELRELELALLVLR---LEELREELEELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAP 1915
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1916 DGSDASQLLHQAEVTQQEFLEvkqRVNSGCVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAVGRDtdsLQSQIED 1995
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1996 VRLFLNKIQVVKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLn 2075
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2076 dattaAEEAEALQWVVGTEVEIINqqladfkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW 2154
Cdd:TIGR02168 512 -----LKNQSGLSGILGVLSELIS-------------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2155 ----------NTLNKKVAQRIAQLQEALLHCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiq 2214
Cdd:TIGR02168 574 tflpldsikgTEIQGNDREILKNIEGFLGVAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT---- 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2215 eqkllqrlLDDRKATVDML------QAEGGRIAQSAELADREKitgQLKSLESRWTELLSKAAARQKQLEDILVLAKQFH 2288
Cdd:TIGR02168 650 --------LDGDLVRPGGVitggsaKTNSSILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2289 ETAEPISDFLSVTEKKLANSE-PVGTQTAKIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDS 2367
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEaEVEQLEERIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2368 LQARYSEIQDRCcrkaALLEQALSNARlfgedevevlnwlAEVEDKLSSVFVKDFKQDVLHKQHADHLALNEEIVNRKKN 2447
Cdd:TIGR02168 787 LEAQIEQLKEEL----KALREALDELR-------------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2448 V-DQAIKNGQALLKQTTGEEVLliQEKLDGIktrytditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAAs 2526
Cdd:TIGR02168 850 LsEDIESLAAEIEELEELIEEL--ESELEAL-----------LNERASLEEALALL---RSELEELSEELRELESKRSE- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2527 ggqsptgeqipqFQQRQKELKKEVMEHRLVLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDA 2606
Cdd:TIGR02168 913 ------------LRRELEELREKLAQLELRLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
890 900 910
....*....|....*....|....*....|....*
gi 1622833258 2607 AIQRSQQYeqaadaelawVAETKRKLMALGPIRLE 2641
Cdd:TIGR02168 966 DEEEARRR----------LKRLENKIKELGPVNLA 990
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
829-1045 |
2.71e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.01 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 829 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 908
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEE---LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 909 KHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLEsLSQSIGEVEQNLEgKQVVSLSSGVIQEALATNMKLK 988
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 989 QDIARQKSSLEATREMVTRFMETADSTTAAVLQGKLAEVSQRFEQLCLQQQEKESSL 1045
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1297-1516 |
3.15e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.01 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1297 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 1376
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1377 KKIEEELNSRWERATEVTVARQRQLEESAGhLASFQAAESQLRPWMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 1456
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1457 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAI 1516
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2878-3050 |
4.78e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 68.24 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2878 ELEKLQPSFEALKRRGEELIgrsqgADKDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEKFWyDMAALLTT 2957
Cdd:cd00176 48 ELAAHEERVEALNELGEQLI-----EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2958 IKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVRKSIDEMNNAWENLNK 3037
Cdd:cd00176 122 LEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
|
170
....*....|...
gi 1622833258 3038 TWKERLEKLEDAM 3050
Cdd:cd00176 201 LAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3493-3595 |
7.27e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 64.66 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3493 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDTQKLDNF 3572
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833258 3573 LGEVRDKWDTVCGKSVERQHKLE 3595
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3165-3266 |
1.21e-11 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 63.88 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3165 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 3244
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
|
90 100
....*....|....*....|..
gi 1622833258 3245 ETMNQCWESVLQKTEEREQQLQ 3266
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLE 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1157-1404 |
9.38e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 64.77 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1157 QLDEFRKLVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapdsqg 1236
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1237 KTGSILPSVGSSvgsvngyhtckDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQkEANSVLQWLESKEEV 1316
Cdd:cd00176 61 ELGEQLIEEGHP-----------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1317 LKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIeEELNSRWERATEVTVA 1396
Cdd:cd00176 129 LASEDLGKDL---ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL-EELNERWEELLELAEE 204
|
....*...
gi 1622833258 1397 RQRQLEES 1404
Cdd:cd00176 205 RQKKLEEA 212
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
3988-4050 |
1.24e-10 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 59.87 E-value: 1.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 3988 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 4050
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
3988-4058 |
1.49e-10 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 62.12 E-value: 1.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622833258 3988 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 4058
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1526-2334 |
4.17e-10 |
|
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: 66.62 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1526 LQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEETS---------EIRSDLEQLDHEVKEAQTLCDELSVLIgeqylkDE 1596
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELElallvlrleELREELEELQEELKEAEEELEELTAEL------QE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1597 LKKRLETVALPLQGLEDlaadRMNRLQAALASTQQFQQMFDElrtwldDKQSQQAKNCPISAKLERLHSQLQENE----E 1672
Cdd:TIGR02168 265 LEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ------QKQILRERLANLERQLEELEAQLEELEskldE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1673 FQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKR-TLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVP 1751
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELeELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1752 WIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQnmdaitee 1831
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1832 LQAKTGSLEEMTQRLKEFQESFKNIEKkvegAKHQLE-IFDALGSQACSNKNLEKlraqqEVLQALEPQVDYLrnftqgL 1910
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLK----NQSGLSgILGVLSELISVDEGYEA-----AIEAALGGRLQAV------V 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1911 VEDAPDGSDASQLLHQAEVTQQEFLEVK----QRVNSGCVMMENKLEGIGQFHCRVREMFSQL-ADLDDELDGMGAVgrd 1985
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFLPLDsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrKALSYLLGGVLVV--- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1986 tDSLQSQIEDVRLFLNKIQVVKLDIEASEAecRHML---EEEGTLDLLGLKRELEALNKQCGKLTER---GKARQEQLEL 2059
Cdd:TIGR02168 629 -DDLDNALELAKKLRPGYRIVTLDGDLVRP--GGVItggSAKTNSSILERRREIEELEEKIEELEEKiaeLEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2060 TLGRVEDFYRKL-KGLNDATTAAEEAEALQWVVGTEVEIINQQLADFKMFQKEQVDPLQMKLQQVNGLGQGLIQSAGKdc 2138
Cdd:TIGR02168 706 ELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-- 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2139 dVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLADTEELIANQkppSAEYKVVKAQIQ---- 2214
Cdd:TIGR02168 784 -IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---EEQIEELSEDIEslaa 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2215 EQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA--DREKITGQLKSLESRWTELLSKAAARQKQLEDI-LVLAK---QFH 2288
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLrsELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGlevRID 939
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1622833258 2289 ETAEPISDFLSVT-EKKLANSEPVGTQTAKIQQQIIRhkaLEEDIEN 2334
Cdd:TIGR02168 940 NLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKR---LENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1954-2852 |
5.79e-10 |
|
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: 66.23 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1954 GIGQFHCRVREMFSQLADLDDELDgmgavgrdtdslqsQIEDVRLFLNKiQVVKLDIEASEAECRHMLEEEG-------- 2025
Cdd:TIGR02168 166 GISKYKERRKETERKLERTRENLD--------------RLEDILNELER-QLKSLERQAEKAERYKELKAELrelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2026 TLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFyrklkglndattaaeeaealqwvvgteveiinqQLADF 2105
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------------------------------RLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2106 KMfqKEQVDPLQMKLQQVNGLgqgliqsagkdcdVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALlhcGKFQDALEPL 2185
Cdd:TIGR02168 278 EL--EEEIEELQKELYALANE-------------ISRLEQQKQILRERLANLERQLEELEAQLEELE---SKLDELAEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2186 LSWLADTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDrkatvdmlQAEGGRIAQSAELADREKITGQLKSLESRwte 2265
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEE--------QLETLRSKVAQLELQIASLNNEIERLEAR--- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2266 lLSKAAARQKQLEdilvlakqfhetaepisdflsvTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKI 2345
Cdd:TIGR02168 409 -LERLEDRRERLQ----------------------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2346 GQslssltspAEQGVLSEKIDSLQARYSEIQDRCcrkaALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVfvkdfkQD 2425
Cdd:TIGR02168 466 LR--------EELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVL------SE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2426 VLHKQHADHLALNEEIVNRKKNV----DQAIKNGQALLKQTTGEEVLLIQekLDGIKtrYTDITVTSSKALRTLEQARQL 2501
Cdd:TIGR02168 528 LISVDEGYEAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRVTFLP--LDSIK--GTEIQGNDREILKNIEGFLGV 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2502 ATKFQSTYEELTGWL--------------------REVEEEL--------------AASGGQSPTG-------------- 2533
Cdd:TIGR02168 604 AKDLVKFDPKLRKALsyllggvlvvddldnalelaKKLRPGYrivtldgdlvrpggVITGGSAKTNssilerrreieele 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2534 EQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLelvpwRAREGLDKLVSDANEQYKLVSDTIGQ---RVDEIDAAIQR 2610
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLR-----KELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTE 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2611 SQQYEQAADAELAWVAETKRKLMAlgpiRLEQDQTTAQlQVQKAFSIDIIRHKDSMDELFSHRSEIFGTcgEEQKTVLQE 2690
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA----EIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANL--RERLESLER 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2691 KTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAE 2770
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEELSEELRE 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2771 HKPHIDKLLKigpQLKELNPEEGEMvEEKYHKAENMYAQIKEEVRQRA-LALDEAVSQSAQITEFHDKIEPMLETLENLS 2849
Cdd:TIGR02168 906 LESKRSELRR---ELEELREKLAQL-ELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 1622833258 2850 SRL 2852
Cdd:TIGR02168 982 KEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1903 |
7.84e-10 |
|
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: 65.46 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1083 ITRFFQQIQELNLEMEDQQENLDTLEHLVTELSScgfALDLSQHQ----DRVQNLRKDFTELQKTV-----KEREKDASS 1153
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELER---QLKSLERQaekaERYKELKAELRELELALlvlrlEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1154 CQEQLDEFRKLVRTFQKWLKETEGSIpptETSMSAK-ELEKQIEHLKSLLDDWAS--------KGTLVEEINCKGTPLEN 1224
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKL---EELRLEVsELEEEIEELQKELYALANeisrleqqKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1225 LIMEITAPDSQ-GKTGSILPSVGSSVGSVNgyhtcKDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQKEA 1303
Cdd:TIGR02168 321 LEAQLEELESKlDELAEELAELEEKLEELK-----EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1304 NSVLQWLESKEEVLKSMDAMSSPTKTETVKAQAESNKAFLAELEQNspkIQKVKEALAGLLVTYPNSQEAenwkkiEEEL 1383
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE---LEELEEELEELQEELERLEEA------LEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1384 NSRWERATEVTVARQRQLEESAGHLASFQAAESQL-------RPWMMEKELMMGVLGPLS----IDP------------- 1439
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvKALLKNQSGLSGILGVLSelisVDEgyeaaieaalggr 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1440 ------NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQId 1513
Cdd:TIGR02168 547 lqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1514 qAIVKS-TQYQELLQDLSEKVRAV---GQRLSGQSAISTQPEAVKQQLEETseiRSDLEQLDHEVKEAQTLCDELSVLIg 1589
Cdd:TIGR02168 626 -LVVDDlDNALELAKKLRPGYRIVtldGDLVRPGGVITGGSAKTNSSILER---RREIEELEEKIEELEEKIAELEKAL- 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1590 eqylkDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQmfdELRTWLDDKQSQQAKNCPISAKLERLHSQLQE 1669
Cdd:TIGR02168 701 -----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---EVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1670 NEEFQKSLNQHSGSYEVIVAEGEslllsvppgEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDL 1749
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLK---------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1750 VPWIEDCKAKMSElrvtldpvqLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAIT 1829
Cdd:TIGR02168 844 EEQIEELSEDIES---------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 1830 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEgAKHQLEIFDALgsqACSNKNLEKLRAQQEVLQALEPQVDYL 1903
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAE---ALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2393-2608 |
9.26e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 61.69 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2393 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 2472
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2473 KLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELaASGGQSPTGEQIPQFQQRQKELKKEVME 2552
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 2553 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 2608
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1421-1626 |
1.23e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 61.31 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1421 WMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSlstSQVQKELQSINQKWVE 1500
Cdd:cd00176 15 WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA---EEIQERLEELNQRWEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1501 LTDKLNSRSTQIDQAIVKSTQYQE---LLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEA 1577
Cdd:cd00176 91 LRELAEERRQRLEEALDLQQFFRDaddLEQWLEEKEAALASEDLGKD-----LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622833258 1578 QTLCDELsVLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRLQAAL 1626
Cdd:cd00176 166 NELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1381-2101 |
1.26e-09 |
|
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: 65.08 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1381 EELNSRWERATEVTVARQRQLEESAGHLASFQAAESQLRPWM----MEKELMMGVLGPLSIDPNMLNAQKQ-------QV 1449
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleEEIEELQKELYALANEISRLEQQKQilrerlaNL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1450 QFMLKEFEARRQQHEQLNEAAQGILTgpgdvslstsQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDL 1529
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1530 SEKVRAVGQRLSGQSAistqpeavkqqleETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKdELKKRLETVAlplQ 1609
Cdd:TIGR02168 385 RSKVAQLELQIASLNN-------------EIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---E 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1610 GLEDLAAdRMNRLQAALASTqqfQQMFDELRTWLDDKQSQQAKncpISAKLERLHSQLQENEEFQKS-----LNQHSGSY 1684
Cdd:TIGR02168 448 ELEELQE-ELERLEEALEEL---REELEEAEQALDAAERELAQ---LQARLDSLERLQENLEGFSEGvkallKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1685 EVIVAegeSLLLSVPPGEEK-------RTLQNQLVELKNHWEE----LSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWI 1753
Cdd:TIGR02168 521 ILGVL---SELISVDEGYEAaieaalgGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1754 EDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSAADI------LINSSEADEDGIRDEKAGI---NQ 1823
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRkALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPGGVITGGSAKTNSSIlerRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1824 NMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQAcsNKNLEKLRAQQE-VLQALEPQVDY 1902
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEqLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1903 LRNFTQGLVEDAPDGSDASQLLHQAEVTQQeflEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQL-ADLDDELDGMGA 1981
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQIEQ----LKEELKALREALDELRAELTLLnEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1982 VGRDTDSLQSQIEDVRlflNKIQVVKLDIEASEAECRHM--LEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLEL 2059
Cdd:TIGR02168 829 LERRIAATERRLEDLE---EQIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1622833258 2060 TLGRVEDFYRKLKGLNDATTAAEEAEAlqwvvGTEVEIINQQ 2101
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLE-----GLEVRIDNLQ 942
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2177-2278 |
2.93e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLE 2278
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3055-3157 |
3.22e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3055 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 3134
Cdd:smart00150 2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833258 3135 LTELKHLWENLGEKIAHRQHKLE 3157
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3384-3485 |
5.05e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.57 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3384 EFQNSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLIKNLL 3463
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 3464 VSVQSRWEKVVQRSIERGRSLD 3485
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2722-2822 |
6.25e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.18 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2722 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 2801
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 2802 KAENMYAQIKEEVRQRALALD 2822
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1630-1733 |
6.50e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.18 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1630 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 1709
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833258 1710 QLVELKNHWEELSKKTADRQSRLK 1733
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2504-2716 |
9.18e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 58.61 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2504 KFQSTYEELTGWLREVEEELAaSGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLELVPWRAREgLDKLV 2583
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2584 SDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAElAWVAETKRKLMALGPIRLEQDqTTAQLQVQKAFSIDIIRHK 2663
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 2664 DSMDELFSHRSEIFGTCGEEQKTVLQEKTESLIQQYEAISLLNSERYARLERA 2716
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
3986-4049 |
1.54e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.80 E-value: 1.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 3986 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 4049
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1738-1942 |
5.45e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 56.30 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1738 KAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDE 1817
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1818 KAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKnIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALE 1897
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622833258 1898 PQVDYLRNFTQGLVEDAPDGSDAsQLLHQAEVTQQEFLEVKQRVN 1942
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAE 203
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3273-3376 |
6.29e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.49 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3273 QGFHSEIEDFLLELTRMESQLSaSKPTGGLPETAREQLDTHMELYSQLKAREETYNQLLDKGRLMLlsRDDSGSGSKTEQ 3352
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833258 3353 SVALLEQKWHAVSSKMEERKSKLE 3376
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
944-1149 |
6.45e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 56.30 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 944 QSVQESLESLSQSIGEVEQNLEGKQVVSLSSGViQEALATNMKLKQDIARQKSSLEATREMVTRFMEtADSTTAAVLQGK 1023
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1024 LAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSgKLQQFMENKSRMLASGNQPD--QDITRFFQQIQELNLEMEDQQ 1101
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622833258 1102 ENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREK 1149
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
3991-4049 |
6.71e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 54.41 E-value: 6.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 3991 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 4049
Cdd:COG5126 37 TLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
320-556 |
7.49e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 55.91 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 320 QLEGRLQDLRAWVGNTILILNSkgSNSETDVDSLNRCLQQYEDLKQPMAERKSQLDALAFDVQFFISEHAQDLSPQQNRq 399
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 400 mlrlLNELQRSFQEILEQTAAQVDALQGHLQQMEQealvktlqkqqntcHQQLEDLCSWVGQAERALAGHQgrtTRQDLS 479
Cdd:cd00176 81 ----LEELNQRWEELRELAEERRQRLEEALDLQQF--------------FRDADDLEQWLEEKEAALASED---LGKDLE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 480 ALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsPHELTALREKLHQAKEQYEALREQTRVAQKELEEA 556
Cdd:cd00176 140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1630-1734 |
9.98e-08 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 52.71 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1630 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 1709
Cdd:pfam00435 4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
|
90 100
....*....|....*....|....*
gi 1622833258 1710 QLVELKNHWEELSKKTADRQSRLKD 1734
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-1179 |
1.16e-07 |
|
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: 58.53 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 347 ETDVDSLNR---CLQQYEDLKQpmAERKSQLDALAFDVQFFISE-HAQDLSPQQNRQMLRLLNELQRSFQEILEQT---- 418
Cdd:TIGR02168 199 ERQLKSLERqaeKAERYKELKA--ELRELELALLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELrlev 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 419 ---AAQVDALQGHLQQM--EQEALVKTLQKQQntchQQLEDLCSWVGQAERALAGHQGR--TTRQDLSALQKNQSDLKDL 491
Cdd:TIGR02168 277 selEEEIEELQKELYALanEISRLEQQKQILR----ERLANLERQLEELEAQLEELESKldELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 492 QDDIQNHATSFAAVVKDIEGFMEENQTklsphELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAA 571
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEE-----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 572 KELAENKKKidALLDWVTSVGSSGGQLLTNLPGMEQ---LSKASLEKGTLDTTDGYMGVNQAPEKLDKhCEKMKARHQEL 648
Cdd:TIGR02168 428 KKLEEAELK--ELQAELEELEEELEELQEELERLEEaleELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 649 lsqqqhfilatQSAQAFLDQHGHNLtPEEQQMLQEKLgELKEQYSTSLaqsEAELKqvQTLQDELQKFLQDHREFESWLE 728
Cdd:TIGR02168 505 -----------SEGVKALLKNQSGL-SGILGVLSELI-SVDEGYEAAI---EAALG--GRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 729 RSEkelenmhKGGSSPEALPSLLKR--QGSFSEDVISHKGDLRFVTIsgqkVLDTENSFKEGKEPSEIGNLVKDKLKDAT 806
Cdd:TIGR02168 567 QNE-------LGRVTFLPLDSIKGTeiQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALSYLLGGVLVVDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 807 ERYTALHSE---CTRLGFHLN---MLLGQYHQFQNSADSLQAWMQTCEANVGKLLSDTVAsdpgvLQQQLATTKQLQEEL 880
Cdd:TIGR02168 636 ELAKKLRPGyriVTLDGDLVRpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE-----LEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 881 AEHqvpVEKLQKVARDImeiegepapdhkhvqettdsilshfqslSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEV 960
Cdd:TIGR02168 711 EEE---LEQLRKELEEL----------------------------SRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 961 EQNLEG-KQVVSLSSGVIQEALATNMKLKQDIARQKSSLEATREMvtrfmetadsttaavlqgkLAEVSQRFEQLCLQQQ 1039
Cdd:TIGR02168 760 EAEIEElEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------------------LDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1040 EKESSLKKLLPQAEMFEHLSGKLQQFMENKSrmlasgnqpdqditrffQQIQELNLEMEDQQENLDTLEHLVTELSScgf 1119
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELEALLN--- 880
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1120 alDLSQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSI 1179
Cdd:TIGR02168 881 --ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3603-3704 |
1.79e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 52.32 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3603 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 3682
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1622833258 3683 ELSTRWDTVCKLSVSKQSRLEQ 3704
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3712-3812 |
1.83e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.95 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3712 FRDTVHMLLEWLSEAEQTLRFRGaLPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWIT 3791
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 3792 IIRARFEEVLTWAKQHQQRLE 3812
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1294-1403 |
1.97e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.94 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1294 NRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 1373
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
|
90 100 110
....*....|....*....|....*....|
gi 1622833258 1374 ENWKKIeEELNSRWERATEVTVARQRQLEE 1403
Cdd:pfam00435 77 EIQERL-EELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1020-1873 |
2.96e-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: 57.00 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1020 LQGKLAEVSQRFEQLCLQQQEKES--SLKKLLPQAEMFEHLsGKLQQFMENKSRMLASGNQPDQDITRFFQQIQELNLEM 1097
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYELL-KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1098 EDQQENLDTLEHLVTELSScgfaldlsqhqdrvqnlrKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEG 1177
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGE------------------EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1178 SIPPTETSMsaKELEKQIEHLKSLLDDWAskgtlvEEINCKGTPLENLIMEITAPDsqgktgsilpsvgssvgsvngyht 1257
Cdd:TIGR02169 330 EIDKLLAEI--EELEREIEEERKRRDKLT------EEYAELKEELEDLRAELEEVD------------------------ 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1258 cKDLTEIQCDMSDVNLKYEKLGgilhERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSmdamssptKTETVKAQAE 1337
Cdd:TIGR02169 378 -KEFAETRDELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEA--------KINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1338 SNKAFLAELEQNSPKIQKVKEALAGLLvtypnSQEAENWKKIEEELNSRwERATEVTVARQRQLEESAGhlaSFQAAEsq 1417
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQEL-----YDLKEEYDRVEKELSKL-QRELAEAEAQARASEERVR---GGRAVE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1418 lrpwMMEKELMMGVLGPLS----IDP-----------NMLNA--------QKQQVQFmLKEFEARRQQHEQLNEAAQ--- 1471
Cdd:TIGR02169 514 ----EVLKASIQGVHGTVAqlgsVGEryataievaagNRLNNvvveddavAKEAIEL-LKRRKAGRATFLPLNKMRDerr 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1472 --GILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRA-VGQRLSGQSAIS- 1547
Cdd:TIGR02169 589 dlSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAmTGGSRAPRGGILf 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1548 --TQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLK-DELKKRLETVALPLQGLEDLAADRMNRLQA 1624
Cdd:TIGR02169 669 srSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKiGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1625 ALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLER--LHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPG- 1701
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEk 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1702 ----EEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ------ 1771
Cdd:TIGR02169 829 eyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieel 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1772 ------LESSLLRSKAMLSEVEKRRSLLEiLNSAADILINSSEADEDGIRDEKAGINQ--------NMDAIT--EELQAK 1835
Cdd:TIGR02169 909 eaqiekKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEeiralepvNMLAIQeyEEVLKR 987
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQRLKEFQESFKNIEKKVEGAKHQ--LEIFDAL 1873
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKKKREvfMEAFEAI 1027
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2945-3047 |
3.01e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.56 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2945 EKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVRKS 3024
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833258 3025 IDEMNNAWENLNKTWKERLEKLE 3047
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
829-937 |
3.64e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.17 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 829 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 908
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
|
90 100
....*....|....*....|....*....
gi 1622833258 909 KHVQETTDSILSHFQSLSYSLAERSSLLQ 937
Cdd:pfam00435 76 EEIQERLEELNERWEQLLELAAERKQKLE 104
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
3991-4050 |
5.96e-07 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 49.53 E-value: 5.96e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 3991 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLemtavADIF---DRDGDGYIDYYEFVAALH 4050
Cdd:cd00052 3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL-----AQIWdlaDTDKDGKLDKEEFAIAMH 60
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2177-2279 |
1.71e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 49.24 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2177 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 2256
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833258 2257 KSLESRWTELLSKAAARQKQLED 2279
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-713 |
1.83e-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: 54.68 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTA-AQVDALQGHLQQMEQEALVKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRT 473
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-----SKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 474 TRQDL----SALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEEnqtklspheLTALREKLHQAKEQYEALREQTRVA 549
Cdd:TIGR02168 766 LEERLeeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE---------LTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 550 QKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLltnlpgMEQLSKASLEKGTLDTTDgymgvnq 629
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEELSEEL------- 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 630 apEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTL 709
Cdd:TIGR02168 904 --RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
....
gi 1622833258 710 QDEL 713
Cdd:TIGR02168 981 IKEL 984
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
874-1622 |
2.30e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 874 KQLQEELAEHQVpVEKLQKVARDI-MEIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLES 952
Cdd:TIGR00618 166 KELLMNLFPLDQ-YTQLALMEFAKkKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 953 LSQSIGEVEQNLE-----GKQVVSLSSGVIQEALATNMKLKQDIARQKSSLEATREMVT--RFMETADSTTAAVLQGKLA 1025
Cdd:TIGR00618 245 LTQKREAQEEQLKkqqllKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTqiEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1026 EVSQRFEQLCLQQQEKES---SLKKLLPQAEMFEHLSGKLQQFMENKSRMLAsgnqpdqdITRFFQQIQELNLEMEDQQE 1102
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEqrrLLQTLHSQEIHIRDAHEVATSIREISCQQHT--------LTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1103 NLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFT-ELQKTVKEREKDASSC--QEQLDEFRKLVRTFQKWlketegsi 1179
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqELQQRYAELCAAAITCtaQCEKLEKIHLQESAQSL-------- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1180 pptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINCKGTPLENLIMEITAPDSQGKTGSILPSVGSS--VGSVNGYH- 1256
Cdd:TIGR00618 469 ---------KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAq 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1257 --TCKDLTEIQCDmSDVNLKYEKLGGILHERQESL------QAILNRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPTK 1328
Cdd:TIGR00618 540 leTSEEDVYHQLT-SERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1329 TETVKAQAESNKAflAELEQNSPKIQKVKEALAGLLVTYPNSQEAENW---KKIEEELNSRWERATEVTVARQRQ----- 1400
Cdd:TIGR00618 619 RKLQPEQDLQDVR--LHLQQCSQELALKLTALHALQLTLTQERVREHAlsiRVLPKELLASRQLALQKMQSEKEQltywk 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1401 --LEESAGHLASFQAAESQLRPWMMEKELMMGVLGplsidpNMLNAQKQQVQFMLKEFEARR--QQHEQLNEAAQGILTG 1476
Cdd:TIGR00618 697 emLAQCQTLLRELETHIEEYDREFNEIENASSSLG------SDLAAREDALNQSLKELMHQArtVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1477 PGDVSLST--SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRA-VGQRLSGQSAISTQpeaV 1553
Cdd:TIGR00618 771 TAALQTGAelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqFLSRLEEKSATLGE---I 847
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 1554 KQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRL 1622
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3380-3486 |
3.19e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 48.47 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3380 NLATEFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLI 3459
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833258 3460 KNLLVSVQSRWEKVVQRSIERGRSLDD 3486
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3493-3596 |
3.51e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 48.47 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3493 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDTQKLDNF 3572
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE--GHYASEEIQER 81
|
90 100
....*....|....*....|....
gi 1622833258 3573 LGEVRDKWDTVCGKSVERQHKLEE 3596
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1297-1402 |
4.89e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1297 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 1376
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833258 1377 KKIEEELNSRWERATEVTVARQRQLE 1402
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-735 |
5.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 385 ISEHAQDLSPQQNRQMLRLLNELQRSFQEI--LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQA 462
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELkeAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 463 ERALAGHQGRTTRQDLS----ALQKNQSDLKDLQDDIQNHATSFAAVVKDIEgfMEENQTKLspheltALREKLHQAKEQ 538
Cdd:COG4717 129 PLYQELEALEAELAELPerleELEERLEELRELEEELEELEAELAELQEELE--ELLEQLSL------ATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 539 YEALREQTRVAQKELEEAVT--SALQQETEKSKAAKELAENKKKIDALLDWVTSVgssGGQLLTNLPGMEQLSKASLEKG 616
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEelEELEEELEQLENELEAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 617 TLDTTDGYMGVnqAPEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHG--HNLTPEEQQMLQEKLGELKEQYSt 694
Cdd:COG4717 278 VLFLVLGLLAL--LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLR- 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622833258 695 SLAQSEAELkQVQTLQDELQKFLQ-----DHREFESWLERSEKELE 735
Cdd:COG4717 355 EAEELEEEL-QLEELEQEIAALLAeagveDEEELRAALEQAEEYQE 399
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2205-2768 |
5.73e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2205 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLKSLESRWTELLSKAAARQKQLEDIL-VL 2283
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2284 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 2357
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2358 QGVLSEKIDSLQARYSEIQDRCCRKAALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHADHLAL 2437
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2438 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYTDIT---------VTSSKALRTLEQARQLATKFQst 2508
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2509 yeELTGWLREVE---EELAASGGQSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 2580
Cdd:COG1196 528 --VLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2581 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 2660
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2661 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 2740
Cdd:COG1196 685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1622833258 2741 IAQLPPPAIDHEQLRQQQEEMRQLRESI 2768
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
395-586 |
6.03e-06 |
|
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: 52.07 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQ-----EALVKTLQKQQNTCHQQLEDLCSWVGQAERALAgh 469
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaalEAELAELEKEIAELRAELEAQKEELAELLRALY-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 470 qgRTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsphELTALREKLHQAKEQYEALREQTRVA 549
Cdd:COG4942 115 --RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA------ELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622833258 550 QKELEEA-------VTSALQQETEKSKAAKELAENKKKIDALLD 586
Cdd:COG4942 187 RAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1276-1867 |
6.35e-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: 52.81 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1276 EKLGGILHERQESLQAIL----NRMEEVQKEANSVLQWLESKEEVLKSmDAMSSPTKTETVKAQAES-NKAFLAELEQNS 1350
Cdd:pfam15921 245 DQLEALKSESQNKIELLLqqhqDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNqNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1351 PKIQKVKEALAGLLVTYPNsqeaenwkKIEEELNSRWERATEVTVAR--QRQLEESAGHL--------ASFQAAESQLRp 1420
Cdd:pfam15921 324 STVSQLRSELREAKRMYED--------KIEELEKQLVLANSELTEARteRDQFSQESGNLddqlqkllADLHKREKELS- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1421 wmMEKELM-------MG---VLGPLSIDPNMLNAQKQQVQFMLKEFEARRQ-QHEQLNEAAQGILTGPGDVSLSTSQvqk 1489
Cdd:pfam15921 395 --LEKEQNkrlwdrdTGnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQ--- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1490 eLQSINQKWVELTDKLNSRSTQIDQAivkSTQYQELLQDLSEKVRAVGqrlSGQSAISTQPEAVKQQLEETSEIRSDLEQ 1569
Cdd:pfam15921 470 -LESTKEMLRKVVEELTAKKMTLESS---ERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQELQHLKNEGDH 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1570 LDHevkeAQTLCDELSVLIGEQylkdelKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQ 1649
Cdd:pfam15921 543 LRN----VQTECEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1650 QAKNcpiSAKLERLHSQLQENEEFQKSLnqhsgsyeviVAEGESLLLSVPPGEEKRtlqNQLV-ELKNHWEELSKKTADR 1728
Cdd:pfam15921 613 KDKK---DAKIRELEARVSDLELEKVKL----------VNAGSERLRAVKDIKQER---DQLLnEVKTSRNELNSLSEDY 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1729 QSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLES--SLLRSKAMLSEVEKRRSLLEILNSAADIL--- 1803
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghAMKVAMGMQKQITAKRGQIDALQSKIQFLeea 756
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 1804 INSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQL 1867
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3825-3949 |
8.85e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3825 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 3903
Cdd:smart00150 7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622833258 3904 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 3949
Cdd:smart00150 78 ----------------------RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2286-2387 |
9.38e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2286 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLSEKI 2365
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEERL 79
|
90 100
....*....|....*....|..
gi 1622833258 2366 DSLQARYSEIQDRCCRKAALLE 2387
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-584 |
1.20e-05 |
|
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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 212 RNIEMRTRQMQPLELNLAELQDLLCQAKVLDRELKDLTTLVSQELECVNqiiisqpqevpaQLLKALEKDAKNLQKSLSS 291
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS------------RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 292 VSDTWNSRllyfqnavEIEKTKVLNQHTQLEGRLQDLRawvgntililnskgsnsetdvDSLNRCLQQYEDLKQPMAERK 371
Cdd:TIGR02168 745 LEERIAQL--------SKELTELEAEIEELEERLEEAE---------------------EELAEAEAEIEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 372 SQLDALafdvqffisehAQDLSPQQNRqmLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTchQQ 451
Cdd:TIGR02168 796 EELKAL-----------REALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA--AE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 452 LEDLCSWVGQAERALAGHQGRTTRQDLsALQKNQSDLKDLQDDIQNhatsfaavvkdiegfMEENQTKLSpHELTALREK 531
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEE-ALALLRSELEELSEELRE---------------LESKRSELR-RELEELREK 923
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622833258 532 LHQAKEQYEALREQ--------TRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDAL 584
Cdd:TIGR02168 924 LAQLELRLEGLEVRidnlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-1151 |
2.73e-05 |
|
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: 50.83 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 415 LEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRttrqdlsaLQKNQSDLKDLQDD 494
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 495 IQNHATSFAAVVKDIEGFMEENQTKLSP-----HELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSK 569
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKldelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 570 AAKELAE-------NKKKIDALLDWVTSVGSSGGQLLTNLpgmEQLSKASLEKGTLDTTDGYMGVNQAPEKLDKHCEKMK 642
Cdd:TIGR02168 384 LRSKVAQlelqiasLNNEIERLEARLERLEDRRERLQQEI---EELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 643 ARHQELLSQQQHFILATQSAQAFLDQHGHNLTPEEQQMLQEK----------------------LGEL---KEQYSTSL- 696
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvLSELisvDEGYEAAIe 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 697 -----------------------AQSEAELKQV----------QTLQDELQKFLQDHREFESWLERSEKELENMHKGGSS 743
Cdd:TIGR02168 541 aalggrlqavvvenlnaakkaiaFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 744 PEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVL----------DTENS-FKEGKEPSEIGNLVKD----------KL 802
Cdd:TIGR02168 621 LLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggvitggsaKTNSSiLERRREIEELEEKIEEleekiaelekAL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 803 KDATERYTALHSECTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEANVgKLLSDTVASDPGVLQQQLATTKQLQEELAE 882
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-AQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 883 HQVPVEKLQKVARDIMEiegepapDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQ 962
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 963 NLEGKQVVSLSSGV----IQEALATNMKLKQDIARQKSSLEATREMVTRFMETADSTTAAvLQGKLAEVSQRFEQLCLQQ 1038
Cdd:TIGR02168 853 DIESLAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSE-LRRELEELREKLAQLELRL 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1039 QEKESSLKKLLPQAEmfEHLSGKLQQFMENKSRMLASGNQPDQDITRFFQQIQEL---NL----EMEDQQENLDTLEHLV 1111
Cdd:TIGR02168 932 EGLEVRIDNLQERLS--EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvNLaaieEYEELKERYDFLTAQK 1009
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1622833258 1112 TELSSCgfaldlsqhqdrVQNLRKDFTELQKTVKEREKDA 1151
Cdd:TIGR02168 1010 EDLTEA------------KETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1707-1895 |
3.98e-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: 50.07 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1707 LQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ-----LESSLLRSK- 1780
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEealndLEARLSHSRi 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1781 ----AMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITE-------ELQAKTGSLEEMTQRLKEF 1849
Cdd:TIGR02169 794 peiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqiksiekEIENLNGKKEELEEELEEL 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622833258 1850 QESFKNIEKKVEGAKHQLEIFDALGSQACSNKN-----LEKLRAQQEVLQA 1895
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEeleaqIEKKRKRLSELKA 924
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
831-937 |
4.08e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 831 HQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDHKH 910
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQ---LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE---EGHPDAEE 74
|
90 100
....*....|....*....|....*..
gi 1622833258 911 VQETTDSILSHFQSLSYSLAERSSLLQ 937
Cdd:smart00150 75 IEERLEELNERWEELKELAEERRQKLE 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2713-2946 |
4.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2713 LERAQVLVNQFWETYEELSPWIEETRALIAQLPPPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 2792
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2793 GEMVEEKYHKAENMyaqikEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipAEVDKIRECISDN 2872
Cdd:PRK03918 265 EERIEELKKEIEEL-----EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------EEINGIEERIKEL 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 2873 KSATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 2946
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1845-2058 |
4.30e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.83 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1845 RLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDgsDASQLL 1924
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1925 HQAEVTQQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQLADLDDELDGMGA--VGRDTDSLQSQIEDVRLFLNK 2002
Cdd:cd00176 79 ERLEELNQRWEELRELAEE----RRQRLEEALDLQQFFRDADDLEQWLEEKEAALASedLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 2003 IQVVKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLE 2058
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1957-2172 |
4.42e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.83 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1957 QFHCRVREMFSQLADLDDELDGMGaVGRDTDSLQSQIEDVRLFLNKIQVVKLDIEASEAECRHMLEEeGTLDLLGLKREL 2036
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2037 EALNKQCGKLTERGKARQEQLELTLGRVEdFYRKLKGLNDATTAAEEAEALQwVVGTEVEIINQQLADFKMFQKEqVDPL 2116
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEE-LEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 2117 QMKLQQVNGLGQGLIQSAGKDcDVQGLEHDMEEINARWNTLNKKVAQRIAQLQEAL 2172
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
551-1203 |
4.80e-05 |
|
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: 50.06 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 551 KELEEAVTSaLQQETEKSKAAKELAENKKKIDALLdWVTSVGSSGGQLLTNLpgmEQLSKASLEKGTLDTTdgymgVNQA 630
Cdd:TIGR02168 196 NELERQLKS-LERQAEKAERYKELKAELRELELAL-LVLRLEELREELEELQ---EELKEAEEELEELTAE-----LQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 631 PEKLDKHCEKMKARHQELLSQQQHFiLATQSAQA-------FLDQHGHNL--TPEEQQMLQEKLGELKEQYSTSLAQSEA 701
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKEL-YALANEISrleqqkqILRERLANLerQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 702 ELKQVQT----LQDELQKFLQDHREFESWLERSEKELENMHKGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQK 777
Cdd:TIGR02168 345 KLEELKEelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 778 VLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSECTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEANVGKLLS- 856
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGf 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 857 -----------DTVASDPGVLQQQLATTKQ----LQEELAEH--QVPVEKLQKVARDI-----------------MEIEG 902
Cdd:TIGR02168 505 segvkallknqSGLSGILGVLSELISVDEGyeaaIEAALGGRlqAVVVENLNAAKKAIaflkqnelgrvtflpldSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 903 EPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVqeslESLSQSIGEVEQNLEGKQVVSL------SSGV 976
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV----DDLDNALELAKKLRPGYRIVTLdgdlvrPGGV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 977 I-QEALATNMKLkqdIARQKSSLEATREMvTRFMETADSTTAAV--LQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAE 1053
Cdd:TIGR02168 661 ItGGSAKTNSSI---LERRREIEELEEKI-EELEEKIAELEKALaeLRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1054 MFEHLSGKLQQFMENKSRMLAsgnQPDQDITRFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGFALD--LSQHQDRVQ 1131
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAELT 813
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833258 1132 NLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMSakELEKQIEHLKSLLD 1203
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE--ELESELEALLNERA 883
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
395-586 |
5.93e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQEAlvKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQgRTT 474
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAE-AEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 475 RQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQTKLSphELTALREKLHQAKEQYEALREQTRVAQKELE 554
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE--ELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
170 180 190
....*....|....*....|....*....|..
gi 1622833258 555 EAVTSALQQETEKSKAAKELAENKKKIDALLD 586
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2682-3394 |
6.67e-05 |
|
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: 49.28 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2682 EEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEM 2761
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL------EQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2762 RQLRESIAEHKPHIDKLLK-----------IGPQLKELNPE---EGEMVEEKYHKAENM---YAQIKEEVRQRALALDEA 2824
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESkldelaeelaeLEEKLEELKEElesLEAELEELEAELEELesrLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2825 VSQ----SAQITEFHDKIEPMLETLENLSSRLR--MPPLIPAEVDKIRECISDNKSatvELEKLQPSFEALKRRGEELIG 2898
Cdd:TIGR02168 392 ELQiaslNNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2899 RSQGADKDL-AAKEIQDKLDQMVFFWEDIKARAEE--REIKFL---------------DVLELAEKFwydMAALLTTI-K 2959
Cdd:TIGR02168 469 ELEEAEQALdAAERELAQLQARLDSLERLQENLEGfsEGVKALlknqsglsgilgvlsELISVDEGY---EAAIEAALgG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2960 DTQDIVHDLESpgidpsiikQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPE-----VRKSIDEMNNAWEN 3034
Cdd:TIGR02168 546 RLQAVVVENLN---------AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgVAKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3035 LNKTWKERL---EKLEDAMQAAVQYQdtLQSMFDWLDNTVIKLCTMpPVGTDLNTVKDQLNEMKEFKvEVYQQQIEMEKL 3111
Cdd:TIGR02168 617 ALSYLLGGVlvvDDLDNALELAKKLR--PGYRIVTLDGDLVRPGGV-ITGGSAKTNSSILERRREIE-ELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3112 NHQGELMLKKATDETDRdiIREPLTELKHLWENLGEKIAHRQHKLEgallALGQFQHALEELMSWLTHTEELLDAQRpis 3191
Cdd:TIGR02168 693 IAELEKALAELRKELEE--LEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLEERIAQLSKELTELEAEI--- 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3192 gdpKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTLQQ 3271
Cdd:TIGR02168 764 ---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-REALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3272 AQGFHSEIEDFLLELTRMESQLSASkptGGLPETAREQLDTHMELYSQLKAREETYNQLLDKgrLMLLSRDDSGSGSKTE 3351
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEEL---EELIEELESELEALLNERASLEEALALLRSELEE--LSEELRELESKRSELR 914
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1622833258 3352 QSVALLEQKWHAVSSKMEERKSKLEEAL-NLATEFQNSLQEFIN 3394
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEA 958
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
804-1640 |
7.32e-05 |
|
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: 49.28 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 804 DATERYTALHSECTRLgfHLNMLLGQYHQFQNSADSLQawmQTCEANVGKLlsDTVASDPGVLQQQLATTK----QLQEE 879
Cdd:TIGR02168 210 EKAERYKELKAELREL--ELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRlevsELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 880 LAEHQ----VPVEKLQKVARDIMEIEGEPAPDHKHVQETTDSILSHFQSLSySLAERSSLLQKAIAQSQSVQESLESLSQ 955
Cdd:TIGR02168 283 IEELQkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-ELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 956 SIGEVEQNLEGK------QVVSLSSGVIQEALATNmKLKQDIARQKSSLEATREMVTRFMETADSTTAAVLQGKLAEVSQ 1029
Cdd:TIGR02168 362 ELEAELEELESRleeleeQLETLRSKVAQLELQIA-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1030 RFEQLCLQQQEKESSLkkllpqAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrfFQQIQELNLEMEDQQENLDTLEH 1109
Cdd:TIGR02168 441 ELEELEEELEELQEEL------ERLEEALEELREELEEAEQALDAAERE--------LAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1110 LVTELSSCgfALDLSQHQDRVQNLRKdFTE-------------LQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETE 1176
Cdd:TIGR02168 507 GVKALLKN--QSGLSGILGVLSELIS-VDEgyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1177 GSIPPTETSM---------SAKELEKQIEHLKSLLDDWASKGTLVEEINC-----KGTPLENLImeITapdsqgKTGSIL 1242
Cdd:TIGR02168 584 TEIQGNDREIlkniegflgVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNalelaKKLRPGYRI--VT------LDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1243 PSVGSSVGSVNGYHTckDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSM-- 1320
Cdd:TIGR02168 656 RPGGVITGGSAKTNS--SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrk 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1321 DAMSSPTKTETVKAQAESNKAFLAELEQ----NSPKIQKVKEALAGLLVTYPNSQE-----AENWKKIEEELNSRWERAT 1391
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAeieeLEERLEEAEEELAEAEAEIEELEAqieqlKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1392 EVTVARQRQLEESAGHLASFQAAESQLRPWMMEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQ 1471
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1472 giltgpgdvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRlsgqsaisTQPE 1551
Cdd:TIGR02168 894 ----------SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--------TLEE 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1552 AvkqqLEETSEIRSDLEQLDHEVKEAQTLCDEL---SVLIGEQYlkDELKKRLETValpLQGLEDLAADRmNRLQAALA- 1627
Cdd:TIGR02168 956 A----EALENKIEDDEEEARRRLKRLENKIKELgpvNLAAIEEY--EELKERYDFL---TAQKEDLTEAK-ETLEEAIEe 1025
|
890
....*....|....*..
gi 1622833258 1628 ----STQQFQQMFDELR 1640
Cdd:TIGR02168 1026 idreARERFKDTFDQVN 1042
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1282-1941 |
7.34e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1282 LHERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPTKteTVKAQAESNKAFLAELEQNSPKI----QKVK 1357
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrarKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1358 EALAGLLVTYPNSQEAENWKKIEEELNSRW-ERATEVTVARQRQ-LEESAGHLASFQAAESQLRPWMMEKELMMGVLGPL 1435
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1436 SIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAqgiltgpgdvslstSQVQKELQSINqkwVELTDKLNSRSTQidqa 1515
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ--------------ATIDTRTSAFR---DLQGQLAHAKKQQ---- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1516 iVKSTQYQELLQDLSEKVRavgqrlsgQSAISTQPEAVK--QQLEETSEIRSDLEQLDHEVKEAQTLcdELSVLIGEQYL 1593
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTA--------QCEKLEKIHLQEsaQSLKEREQQLQTKEQIHLQETRKKAV--VLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1594 KDELKKRLETVALPLQGLEDLAADrMNRLQAALASTQQFQQMFDELRTWLDDKQSQqakncpisakLERLHSQLQENEEF 1673
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPL-TRRMQRGEQTYAQLETSEEDVYHQLTSERKQ----------RASLKEQMQEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1674 QKSLNQHSGSYEVIVAEGESLLLSVPP-GEEKRTLQNQLV-ELKNHWEELSKKTADRQSRLKD--CMQKAQKYQWHVEDL 1749
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDlTEKLSEAEDMLAcEQHALLRKLQPEQDLQDVRLHLqqCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1750 VPWIEDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSaADILINSSEADEDGIRDEKAGINQNMDAI 1828
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQ-CQTLLRELETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1829 TEELQAKTGSLEEMTQRLK-EFQESFKNIEKKVEGAKHQLEIFDALGSQacsnknLEKLRAQQEVLQ-ALEPQVDYLRNF 1906
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMhQARTVLKARTEAHFNNNEEVTAALQTGAE------LSHLAAEIQFFNrLREEDTHLLKTL 804
|
650 660 670
....*....|....*....|....*....|....*
gi 1622833258 1907 TQGLVEDAPDGSDAsqLLHQAEVTQQEFLEVKQRV 1941
Cdd:TIGR00618 805 EAEIGQEIPSDEDI--LNLQCETLVQEEEQFLSRL 837
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3719-3812 |
8.53e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 44.62 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3719 LLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWITIIRARFE 3798
Cdd:pfam00435 13 LESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWE 90
|
90
....*....|....
gi 1622833258 3799 EVLTWAKQHQQRLE 3812
Cdd:pfam00435 91 QLLELAAERKQKLE 104
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
4000-4049 |
8.62e-05 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 43.07 E-value: 8.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622833258 4000 QDGKITRQEFIDGILASKFP-TTKLEMTAVADIFDRDGDGYIDYYEFVAAL 4049
Cdd:pfam13833 1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
373-584 |
9.67e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 373 QLDALAFDVQ----------FFISEH---AQDLSPQQNRQMLRL-LNELQR---SFQEILEQTAAQVDALQGHLQQME-- 433
Cdd:COG3096 800 QYAKASFDVQklqrlhqafsQFVGGHlavAFAPDPEAELAALRQrRSELERelaQHRAQEQQLRQQLDQLKEQLQLLNkl 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 434 --QEALVK--TLQKQQNTCHQQLEDLcswvGQAERALAGHQGRTTR------------QDLSALQKNQSDLKDLQDDIQN 497
Cdd:COG3096 880 lpQANLLAdeTLADRLEELREELDAA----QEAQAFIQQHGKALAQleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQ 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 498 HATSFAAVVK--------DIEGFMEENQTkLSPheltALREKLHQAKEQYEALREQTRVAQKELEEAvtSALQQETEKSK 569
Cdd:COG3096 956 QIFALSEVVQrrphfsyeDAVGLLGENSD-LNE----KLRARLEQAEEARREAREQLRQAQAQYSQY--NQVLASLKSSR 1028
|
250
....*....|....*..
gi 1622833258 570 AAK--ELAENKKKIDAL 584
Cdd:COG3096 1029 DAKqqTLQELEQELEEL 1045
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2942-3048 |
1.10e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 44.23 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2942 ELAEKFWYDMAALLTTIKDTQDIVHDlESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFAcGETEKPEV 3021
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833258 3022 RKSIDEMNNAWENLNKTWKERLEKLED 3048
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1051-1293 |
1.25e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 46.28 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1051 QAEMFEHLSGKLQQFMENKSRMLASGNQPD--QDITRFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGfALDLSQHQD 1128
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDdlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1129 RVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKlVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASK 1208
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1209 GTLVEEINCKGTPLENLimeitapdsqgktgsilpsvgssvgsvngyHTCKDLTEIQCDMSDVNLKYEKLGGILHERQES 1288
Cdd:cd00176 159 EPRLKSLNELAEELLEE------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
....*
gi 1622833258 1289 LQAIL 1293
Cdd:cd00176 209 LEEAL 213
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1484-1861 |
1.35e-04 |
|
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: 48.09 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1484 TSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSGQSA----ISTQPEAVKQQLEE 1559
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1560 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRMNRLQAALASTQQFQQMFD 1637
Cdd:TIGR04523 307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1638 ELRTWLDDKQSQQAKNCPISAKLERLHSQLQE----NEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 1712
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1713 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSE 1785
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 1786 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVE 1861
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
412-586 |
1.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 412 QEILEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTRQdLSALQKNQSDLKDL 491
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEE--YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 492 qdDIQNHATSFAAVVKDIEG---FMEENQTKLSphELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKS 568
Cdd:COG3883 106 --DVLLGSESFSDFLDRLSAlskIADADADLLE--ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170
....*....|....*...
gi 1622833258 569 KAAKELAENKKKIDALLD 586
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLA 199
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2728-2823 |
1.64e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.85 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2728 EELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYHKAENMY 2807
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
|
90
....*....|....*.
gi 1622833258 2808 AQIKEEVRQRALALDE 2823
Cdd:pfam00435 90 EQLLELAAERKQKLEE 105
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
398-583 |
2.05e-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: 46.07 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 398 RQMLRLLNELQRSFQEIlEQTAAQVDALQGHLQQMEQEalVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTR-Q 476
Cdd:COG1579 3 PEDLRALLDLQELDSEL-DRLEHRLKELPAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 477 DLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEEnqtklspheLTALREKLHQAKEQYEALREQTRVAQKELEEA 556
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER---------IEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....*..
gi 1622833258 557 VTSALQQETEKSKAAKELAenkKKIDA 583
Cdd:COG1579 151 LAELEAELEELEAEREELA---AKIPP 174
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3055-3157 |
2.09e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.46 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3055 QYQDTLQSMFDWLDNTVIKLcTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 3134
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
|
90 100
....*....|....*....|...
gi 1622833258 3135 LTELKHLWENLGEKIAHRQHKLE 3157
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLE 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
395-586 |
2.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQEALVktlqkqqntcHQQLEDLcSW----VGQAERALAghq 470
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA----------LQRLAEY-SWdeidVASAEREIA--- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 471 grTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGfMEENQTKLSpHELTALREKLHQAKEQYEALREQTRVAQ 550
Cdd:COG4913 672 --ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE-LKGEIGRLE-KELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622833258 551 KE-LEEAVTSALQQETEKsKAAKELAENKKKIDALLD 586
Cdd:COG4913 748 RAlLEERFAAALGDAVER-ELRENLEERIDALRARLN 783
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1737-1841 |
2.15e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.46 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1737 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRD 1816
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1622833258 1817 EKAGINQNMDAITEELQAKTGSLEE 1841
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
358-584 |
2.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 358 QQYEDLKQPMAERKSQLDALAFDVQ----------FFISEHAQ---DLSPQQNRQMLRL-LNELQRSFQEILEQT---AA 420
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQklqrlhqafsRFIGSHLAvafEADPEAELRQLNRrRVELERALADHESQEqqqRS 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 421 QVDALQGHLQQMEQEA------LVKTLQKQQNTCHQQLEDLcswvGQAERALAGHQGRTTR--QDLSALQKNQSDLKDLQ 492
Cdd:PRK04863 866 QLEQAKEGLSALNRLLprlnllADETLADRVEEIREQLDEA----EEAKRFVQQHGNALAQlePIVSVLQSDPEQFEQLK 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 493 DD----------IQNHATSFAAVVK--------DIEGFMEENQtKLSPheltALREKLHQAKEQYEALREQTRVAQKELE 554
Cdd:PRK04863 942 QDyqqaqqtqrdAKQQAFALTEVVQrrahfsyeDAAEMLAKNS-DLNE----KLRQRLEQAEQERTRAREQLRQAQAQLA 1016
|
250 260 270
....*....|....*....|....*....|..
gi 1622833258 555 EA--VTSALQqeTEKSKAAKELAENKKKIDAL 584
Cdd:PRK04863 1017 QYnqVLASLK--SSYDAKRQMLQELKQELQDL 1046
|
|
| EFh_PEF_ALG-2_like |
cd16185 |
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
3992-4050 |
2.39e-04 |
|
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).
Pssm-ID: 320060 [Multi-domain] Cd Length: 163 Bit Score: 44.51 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3992 FFRRIDKDQDGKITRQEfIDGILASKFPTTKLEMTA-VADIFDRDGDGYIDYYEFvAALH 4050
Cdd:cd16185 5 WFRAVDRDRSGSIDVNE-LQKALAGGGLLFSLATAEkLIRMFDRDGNGTIDFEEF-AALH 62
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2682-2932 |
2.55e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.14 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2682 EEQKTVLQEKTESLIQQYEAisllNSERYARLE------RAQVLVN--QFWETYEELSPWIEETRALIAQL--------P 2745
Cdd:PRK04778 118 EEDIEQILEELQELLESEEK----NREEVEQLKdlyrelRKSLLANrfSFGPALDELEKQLENLEEEFSQFveltesgdY 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2746 PPAidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGP-QLKELnpEEG--EMVEEKYH----KAENMYAQIKEEVRQ-- 2816
Cdd:PRK04778 194 VEA--REILDQLEEELAALEQIMEEIPELLKELQTELPdQLQEL--KAGyrELVEEGYHldhlDIEKEIQDLKEQIDEnl 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2817 ---RALALDEAvsqSAQITEFHDKIEPMLETLEN-LSSRLRMPPLIPAEVDKIRECISDNKSATVELEKLQPSFE----- 2887
Cdd:PRK04778 270 allEELDLDEA---EEKNEEIQERIDQLYDILEReVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTlnese 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 2888 -----ALKRRGEELIGRSQGADKDLAAK-----EIQDKLDQMVFFWEDIKARAEE 2932
Cdd:PRK04778 347 lesvrQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEK 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
395-1103 |
3.32e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQEALVKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQG-RT 473
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 474 TRQDLSALQKNQSDLKDLQDDIQNHATSFAAVV---KDIEGFMEENQTKLSPHELTALREKLH---QAKEQYEALREQTR 547
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafRDLQGQLAHAKKQQELQQRYAELCAAAitcTAQCEKLEKIHLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 548 VAQK-----ELEEAVTSALQQETEKSKAAKELAENKKKIDALLDWVTSVGSSGGQLLTNLPGMEQLSKASLekgtldttD 622
Cdd:TIGR00618 464 SAQSlkereQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE--------Q 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 623 GYMGVNQAPEKLDKHCEKMKARHQELLSQQQHfILATQSAQAFLDQHGHNLTPEEQQMLQEKLGELKEQysTSLAQSEAE 702
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQE-IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL--SEAEDMLAC 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 703 LKQVQTLQDELQKFLQDHREFESWLERSEKElenmhkggsspeALPSLLKRQGSFSEDVISHKgdLRFVTISgQKVLDTE 782
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREH--ALSIRVL-PKELLAS 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 783 NSFKEGKEPSEIGNLVKDKlKDATERYTALHSECTrlgfHLNMLLGQYHQFQNSADSLQAwmqtceanvgkllsdtvasd 862
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWK-EMLAQCQTLLRELET----HIEEYDREFNEIENASSSLGS-------------------- 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 863 pgVLQQQLATTKQLQEELaEHQVPVEKLQKVARDIMEIEGEPApdhkhvqettdsilshfqsLSYSLAERSSLLQKAIAQ 942
Cdd:TIGR00618 733 --DLAAREDALNQSLKEL-MHQARTVLKARTEAHFNNNEEVTA-------------------ALQTGAELSHLAAEIQFF 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 943 SQSVQESLESLSQSIGEVEQNLEGKQvvslssgviQEALATNMKLKQDIARQKSSLEatremvtrfMETADSTTAAVLQG 1022
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDE---------DILNLQCETLVQEEEQFLSRLE---------EKSATLGEITHQLL 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1023 KLAEVSQRFEQLCLQQQEKESSLKKLlpqaemfEHLSGKLQQFMENKSRMLASGNQPDQDITRFFQQIQELNLEMEDQQE 1102
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL-------NGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHV 925
|
.
gi 1622833258 1103 N 1103
Cdd:TIGR00618 926 N 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
987-1319 |
3.80e-04 |
|
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: 46.98 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 987 LKQDIARQKSSL-EATREM--VTRFMETAdSTTAAVLQGKLAEVSQRFEQLCLQQQEKEsslKKLLPQAEMFEHLSGKLQ 1063
Cdd:TIGR02169 693 LQSELRRIENRLdELSQELsdASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1064 QFMENKSRMLASGNQPDQDITRffQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLSQHQDRVQNLRKDFTELQKT 1143
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1144 VKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMsaKELEKQIEHLKSLLDDWASK-GTLVEEINCKG--- 1219
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--GDLKKERDELEAQLRELERKiEELEAQIEKKRkrl 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1220 ----TPLENLIMEITAPDSQGKTGSILPSVGSSVGSVngYHTCKDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNR 1295
Cdd:TIGR02169 920 selkAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
330 340
....*....|....*....|....
gi 1622833258 1296 MEEvqkEANSVLQWLESKEEVLKS 1319
Cdd:TIGR02169 998 LEE---ERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1440-1997 |
3.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1440 NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTgpgdvslSTSQVQKELQSINQKWVELTDKL----NSRSTQIDQA 1515
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLE-------EHEERREELETLEAEIEDLRETIaeteREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1516 IVKSTQYQELLQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEETSE------------------IRSDLEQLDHEVKEA 1577
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleecrvaaqahneeaesLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1578 QTLCDELSVLIgeQYLKDELKKRLETVAlplqGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpIS 1657
Cdd:PRK02224 362 REEAAELESEL--EEAREAVEDRREEIE----ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE---LE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1658 AKLERLHSQLQENEEFQKSLNQHSGSYEVivaEGESLLLSVPPGEEKR-TLQNQLVELKNHWEELSKKTaDRQSRLKDCM 1736
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPV---EGSPHVETIEEDRERVeELEAELEDLEEEVEEVEERL-ERAEDLVEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1737 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAmlseVEKRrslleilNSAADILINSSEAdedgiRD 1816
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA----EEKR-------EAAAEAEEEAEEA-----RE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1817 EKAGINQNMDAITEELQaktgSLEemtqRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQacsnkNLEKLRAQQEVLQAL 1896
Cdd:PRK02224 573 EVAELNSKLAELKERIE----SLE----RIRTLLAAIADAEDEIERLREKREALAELNDE-----RRERLAEKRERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1897 EPQVDYLRnftqglVEDA-PDGSDASQLLHQAEVTQQEFLEVKQRVNSGCVMMENKLEgigqfhcRVREMFSQLADLDDE 1975
Cdd:PRK02224 640 EAEFDEAR------IEEArEDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------ELEELRERREALENR 706
|
570 580
....*....|....*....|..
gi 1622833258 1976 LDGMGAVGRDTDSLQSQIEDVR 1997
Cdd:PRK02224 707 VEALEALYDEAEELESMYGDLR 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2479-3332 |
6.16e-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: 46.20 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2479 TRYTDITVTSSKALRTLEQARQLATKFQstyeELTGWLREVEEELAASggqsptgeQIPQFQQRQKELKKEVMEHRLVLD 2558
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYK----ELKAELRELELALLVL--------RLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2559 TVNEVSRALLELVpwrarEGLDKLVSDANEQYklvsDTIGQRVDEIDAAIQRSQQYEQAADAELAwvaetkrklmalgpi 2638
Cdd:TIGR02168 257 ELTAELQELEEKL-----EELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLA--------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2639 RLEQDQTTAQLQVQKAFSiDIIRHKDSMDELfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQV 2718
Cdd:TIGR02168 313 NLERQLEELEAQLEELES-KLDELAEELAEL------------EEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2719 LVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAEH--KPHIDKLLKIGPQLKELNPEEgEMV 2796
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERL------EARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEEL-EEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2797 EEKYHKAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipaEVDKIRECISDNKSAT 2876
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK-------ALLKNQSGLSGILGVL 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2877 VELEKLQPSFE-----ALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFF----WEDIKARAEEREIK-----FLDVLE 2942
Cdd:TIGR02168 526 SELISVDEGYEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLpldsIKGTEIQGNDREILkniegFLGVAK 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2943 LAEKFWYDMAALLTTIKDTQDIVHDLESpgidpsiikqqveAAETIKEetdgLHEELEFIrILGADLIFACG-------- 3014
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGGVLVVDDLDN-------------ALELAKK----LRPGYRIV-TLDGDLVRPGGvitggsak 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3015 --------ETEKPEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSMFDWLDNTVIKLctmppvgtdlnt 3086
Cdd:TIGR02168 668 tnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL------------ 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3087 vkdqlnEMKEFKVEVYQQQIEMEKLNhQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQF 3166
Cdd:TIGR02168 736 ------ARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3167 QHALEEL-MSWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLE---------SSAGDD 3236
Cdd:TIGR02168 809 RAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnerASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3237 ASSLRSRLETMnqcwESVLQKTEEREQQLQSTLQQAQgfhSEIEDFLLELTRMESQLSaskptgGLPETAREQLDTHMEL 3316
Cdd:TIGR02168 889 LALLRSELEEL----SEELRELESKRSELRRELEELR---EKLAQLELRLEGLEVRID------NLQERLSEEYSLTLEE 955
|
890
....*....|....*.
gi 1622833258 3317 YSQLKAREETYNQLLD 3332
Cdd:TIGR02168 956 AEALENKIEDDEEEAR 971
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2686-2946 |
6.47e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2686 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpppaidhEQLR 2755
Cdd:COG0497 116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2756 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYHKAENmYAQIKEEVRQRALALDE------ 2823
Cdd:COG0497 179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2824 -----AVSQSAQITEFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 2888
Cdd:COG0497 244 dllgqALRALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833258 2889 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 2946
Cdd:COG0497 311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
358-1034 |
6.75e-04 |
|
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: 46.26 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 358 QQYEDLKQPMAERKSQLDALAfdvqffisehaqDLSPQQNRQMLRLLNELQRSFQEILEQTAAQVDALQGHLQQMEQeaL 437
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMA------------DIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQ--L 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 438 VKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTT---RQDLSALQKNqsdLKDLQDDIQNHATSFAAVVKDIEGFME 514
Cdd:pfam15921 176 RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfRSLGSAISKI---LRELDTEISYLKGRIFPVEDQLEALKS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 515 ENQTKL---------------SPHE--LTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQ----ETEKSKAAKE 573
Cdd:pfam15921 253 ESQNKIelllqqhqdrieqliSEHEveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQlsdlESTVSQLRSE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 574 LAENKK----KIDALLDWVTSVGSSGGQLLTNlpgMEQLSKaslEKGTLDttdgymgvnqapEKLDKHCEKMKARHQEL- 648
Cdd:pfam15921 333 LREAKRmyedKIEELEKQLVLANSELTEARTE---RDQFSQ---ESGNLD------------DQLQKLLADLHKREKELs 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 649 LSQQQHFILATQ-SAQAFLDQHGHNLTPEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHREFESWL 727
Cdd:pfam15921 395 LEKEQNKRLWDRdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 728 ERSEKELENMHKGGSSPEAlpsllkrqgsfSEDVIShkgdlrfvtisgqkvlDTENSFKEgkepseignlvKDKLKDATe 807
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLES-----------SERTVS----------------DLTASLQE-----------KERAIEAT- 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 808 rytalHSECTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEA---------NVGKLLSDTVASDPGVLQQQ-------LA 871
Cdd:pfam15921 516 -----NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlklqmaekdKVIEILRQQIENMTQLVGQHgrtagamQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 872 TTKQLQEELAEHQVPVEKLqKVARD-----IMEIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAiaqsQSV 946
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEF-KILKDkkdakIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV----KTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 947 QESLESLSQSIGEVEQNLEGKQvvslssgviQEALATNMKLKQDIARQKSSLEATREMVtRFMETADSTTAAVLQGKLAE 1026
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKS---------EEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHAMKVAMGMQKQ 735
|
....*...
gi 1622833258 1027 VSQRFEQL 1034
Cdd:pfam15921 736 ITAKRGQI 743
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
479-777 |
7.13e-04 |
|
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: 45.53 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 479 SALQKNQSDLKDLQDDIQNHATSFAAvvkdiegfmEENQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAvt 558
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 559 salqqETEKSKAAKELAENKKKIDALLDWVtsvgssggQLLTNLPGMEQLSKASlekGTLDTTDGYMGVNQAPEKLDKHC 638
Cdd:COG4942 89 -----EKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 639 EKMKARHQELLSQQQHFILATQSAQAFLDqhghnltpeEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQ 718
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLA---------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833258 719 DHREFESWLERSEKELENMHKGGSSPEA-----LP---SLLKRQGSFSEDVISHKGdlrfVTISGQK 777
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALkgklpWPvsgRVVRRFGERDGGGGRNKG----IDIAAPP 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-1348 |
7.92e-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: 45.82 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 416 EQTAAQVDALQGHLQQMEqeALVKTLQKQQNTCHQQLEdlcswvgQAERALAGH-QGRTTRQDLSALQKNQsdLKDLQDD 494
Cdd:TIGR02168 175 KETERKLERTRENLDRLE--DILNELERQLKSLERQAE-------KAERYKELKaELRELELALLVLRLEE--LREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 495 IQNHATSFAAVVKDIEGFMEENQTKLSPHEL--TALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAK 572
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 573 ELAENKKKIDALLDWVTSVGSSGGQLLTNLPGM-EQLSKASLEKGTLdttdgymgvNQAPEKLDKHCEKMKARHQELLSQ 651
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLeAELEELEAELEEL---------ESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 652 QQhfilATQSAQAFLDQHGHNLTPEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHREFESWLERSE 731
Cdd:TIGR02168 395 IA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 732 KELEN--------MHKGGSSPEALPSLLKRQGSFSEDVIshkgdlrfvtisgqkvldteNSFKEGKEPSEIGNLVKDKLK 803
Cdd:TIGR02168 471 EEAEQaldaaereLAQLQARLDSLERLQENLEGFSEGVK--------------------ALLKNQSGLSGILGVLSELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 804 DATERYTALHsecTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEANVGKLLSDTVASDPGVLQQQLATTKQLQEELAEH 883
Cdd:TIGR02168 531 VDEGYEAAIE---AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 884 QVPVEKLQKVARDIMeiegepapDHKHVQETTDSILShfQSLSYSLAERSSLLQKAIAQSQ-SVQESLESLSQSIGEVEQ 962
Cdd:TIGR02168 608 VKFDPKLRKALSYLL--------GGVLVVDDLDNALE--LAKKLRPGYRIVTLDGDLVRPGgVITGGSAKTNSSILERRR 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 963 NLEgkqvvslssgviqealatnmKLKQDIARQKSSLEATRemvtrfmetadsTTAAVLQGKLAEVSQRFEQLCLQQQEKE 1042
Cdd:TIGR02168 678 EIE--------------------ELEEKIEELEEKIAELE------------KALAELRKELEELEEELEQLRKELEELS 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1043 SSLKKLLPQAEMFEHLSGKLQQFMEnksrmlasgnQPDQDITRFFQQIQELNLEMEDQQENLDTLEhlvtelsscgfald 1122
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIA----------QLSKELTELEAEIEELEERLEEAEEELAEAE-------------- 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1123 lsqhqdrvqnlrKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT-----FQKWLKETEGSIPPTETSMSAKELEKQI-- 1195
Cdd:TIGR02168 782 ------------AEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERLESLERRIAATERRLEDLEEQIee 849
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1196 --EHLKSLLDDWASKGTLVEEINCKGTPLENLIMEITAPDSQGKtgsilpsvgssvgsvngyhtcKDLTEIQCDMSDVNL 1273
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR---------------------SELEELSEELRELES 908
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833258 1274 KYEKLGGILHERQESLQAILNRMEEVQKEANSVLQWLESKEevlkSMDAMSSPTKTETVKAQAESNKAFLAELEQ 1348
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY----SLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2286-2388 |
8.55e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 41.54 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2286 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLtSPAEQGVLSEKI 2365
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833258 2366 DSLQARYSEIQDRCCRKAALLEQ 2388
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
234-733 |
1.27e-03 |
|
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: 45.10 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 234 LLCQAKVLDRELKDLTTLVSQELECVNQiiISQPQEVPAQLLKALEKDAKNLQKSLSSVSDTWNsRLLYFQNAVEIE--- 310
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQ--LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-RSMSTQKALEEDlqi 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 311 KTKVLNQHT-QLEGRLQDL-RAWVGNTILIlnskgSNSETDVDSLNRCLQQYEdlkQPMAERKSQLDALAFDVQFFISEH 388
Cdd:pfam05483 322 ATKTICQLTeEKEAQMEELnKAKAAHSFVV-----TEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 389 AQDLSPQQNRQM-LRLLNELQRSFQEILEQTaAQVDALQGHLQQMEQEaLVKTLQKQQNTCH-----------------Q 450
Cdd:pfam05483 394 EEMTKFKNNKEVeLEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQE-LIFLLQAREKEIHdleiqltaiktseehylK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 451 QLEDLCSWVGQAE---RALAGHQGRTTRQDLSALQKNQS---DLKDLQDDIQNHATSFAAVVKDIEGfMEENQTKLSpHE 524
Cdd:pfam05483 472 EVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLR-DE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 525 LTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQET---EKSKAAKELAENKKK-IDALLDWVTSVGSSGGQLLT 600
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKileNKCNNLKKQIENKNKnIEELHQENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 601 NLPGME------QLSKASLEKGTLDTTDGYMGVNQ----APEKLDKHCEKMKARHQELLSQQQHFILATQ----SAQAFL 666
Cdd:pfam05483 630 QLNAYEikvnklELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaEMVALM 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833258 667 DQHGHnltpEEQQMLQEKLGEL-----KEQYSTSLAQS-EAELKQVQTLQDELQKFLQDHREFESWLERSEKE 733
Cdd:pfam05483 710 EKHKH----QYDKIIEERDSELglyknKEQEQSSAKAAlEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2210-3140 |
1.85e-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: 44.67 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2210 KAQIQEQKLLQRLLDDRKATVDMLQAEggriaqsAELADREKITGQLKSLESRWTELLSKAAARQKQLEDILVLAKQFHE 2289
Cdd:TIGR02169 207 REKAERYQALLKEKREYEGYELLKEKE-------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2290 TAEPISDFLSVTekklansepVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQS-LSSLTSPAEQgvLSEKIDSL 2368
Cdd:TIGR02169 280 KIKDLGEEEQLR---------VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAeIDKLLAEIEE--LEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2369 QARYSEIQDRCCRKAALLEQALSNArlfGEDEVEvlnwLAEVEDKLSSVFVKdfkQDVLHKQHADHLALNEEIVNRKKNV 2448
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAEL---EEVDKE----FAETRDELKDYREK---LEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2449 DQAIKNGQALLKQttgeevllIQEKLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTYEELTGWLREVEEELAASgg 2528
Cdd:TIGR02169 419 SEELADLNAAIAG--------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2529 qsptGEQIPQFQQRQKELKKEVMEHRLVLDTVNEvsrallelvpwrAREGLDKLVSD---ANEQYKL-VSDTIGQRVDEI 2604
Cdd:TIGR02169 489 ----QRELAEAEAQARASEERVRGGRAVEEVLKA------------SIQGVHGTVAQlgsVGERYATaIEVAAGNRLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2605 ----DAAIQRSQQY---EQAADAELAWVAETKRKLMALGPIRLEQdqttaqlqvQKAFSIDIIRHKDSMDELFSHrseIF 2677
Cdd:TIGR02169 553 vvedDAVAKEAIELlkrRKAGRATFLPLNKMRDERRDLSILSEDG---------VIGFAVDLVEFDPKYEPAFKY---VF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2678 GTcgeeqkTVLQEKTES---LIQQYEAISL---------LNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLp 2745
Cdd:TIGR02169 621 GD------TLVVEDIEAarrLMGKYRMVTLegelfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2746 ppaidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKigpQLKELNPEEGEMVEEkyhkAENMYAQIKEEVRQRALALDEAV 2825
Cdd:TIGR02169 694 -----QSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKER----LEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2826 SQSAQITEFHDKIEPMLETLENLSSRLRMPPL--IPAEVDKIRECISDNKSATVELEKlqpsfeALKRRGEEligrsqga 2903
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIEQ------KLNRLTLE-------- 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2904 dKDLAAKEIQDKLDQMvffwEDIKARAEEREikflDVLELAEKFwydMAALLTTIKDTQDIVHDLESPGIDpsiikqqve 2983
Cdd:TIGR02169 828 -KEYLEKEIQELQEQR----IDLKEQIKSIE----KEIENLNGK---KEELEEELEELEAALRDLESRLGD--------- 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2984 aaetIKEETDGLHEELEfirilgadlifacgetekpEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSM 3063
Cdd:TIGR02169 887 ----LKKERDELEAQLR-------------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3064 FDwldntviklctMPPVGTDLNTVKDQLNEMKE---------FKVEvyqQQIEmEKLNHQGELMLKKATDETDRDIIR-- 3132
Cdd:TIGR02169 944 EE-----------IPEEELSLEDVQAELQRVEEeiralepvnMLAI---QEYE-EVLKRLDELKEKRAKLEEERKAILer 1008
|
....*....
gi 1622833258 3133 -EPLTELKH 3140
Cdd:TIGR02169 1009 iEEYEKKKR 1017
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
449-554 |
1.91e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 449 HQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENqtklsPHELTAL 528
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833258 529 REKLHQAKEQYEALREQTRVAQKELE 554
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| EFh_CREC_RCN3 |
cd16230 |
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ... |
3993-4050 |
1.99e-03 |
|
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.
Pssm-ID: 320028 [Multi-domain] Cd Length: 268 Bit Score: 43.42 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 3993 FRRIDKDQDGKITRQEFIDGILASKFPTTK-LEMTAVADIFDRDGDGYIDYYEFVAALH 4050
Cdd:cd16230 129 FRVADQDGDSMATREELTAFLHPEEFPHMRdIVVAETLEDLDKNKDGYVQVEEYIADLY 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1446-1864 |
2.39e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1446 KQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQEL 1525
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1526 LQDLSEKVRAVGQRL---SGQSAISTQPEAVKQQLEETSEIRSDL-----------EQLDHEVKEAQTLCDELSVLIGE- 1590
Cdd:TIGR00606 614 LESKEEQLSSYEDKLfdvCGSQDEESDLERLKEEIEKSSKQRAMLagatavysqfiTQLTDENQSCCPVCQRVFQTEAEl 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1591 QYLKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSqqaKNCPISAKLERLHSQLQEN 1670
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRN---KLQKVNRDIQRLKNDIEEQ 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1671 EEFQKSLNQHSGSYEV------IVAEGESLLLSVPPGEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQW 1744
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVcltdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1745 HVEDLVPWIEDCKAKMSELRVtlDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQN 1824
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKS--EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622833258 1825 MDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAK 1864
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1388-1895 |
2.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1388 ERATEVTVARQRQLEESAGHLASFQAAESQLRPwmMEKELmmgvlgplsidpnmlnAQKQQVQFMLKEFEAR-------- 1459
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LEQRL----------------RQQQRAERLLAEFCKRlgknldde 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1460 ------RQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQ-------SINQKWVELTDKLNSRSTQIDQAIVKSTQYQELL 1526
Cdd:PRK04863 554 deleqlQEELEARLESLSESVSEARERRMALRQQLEQLQariqrlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYM 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1527 QDLSEKVRAVGQRLSGqsaISTQPEAVKQQLEETSEIR-SDLEQLdhevkeaQTLCDELS-VLIGEQY----LKDE---- 1596
Cdd:PRK04863 634 QQLLERERELTVERDE---LAARKQALDEEIERLSQPGgSEDPRL-------NALAERFGgVLLSEIYddvsLEDApyfs 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1597 ----------LKKRLETVALPLQGLEDLAAD-----------RMNRLQAAL---ASTQQF-------------------- 1632
Cdd:PRK04863 704 alygparhaiVVPDLSDAAEQLAGLEDCPEDlyliegdpdsfDDSVFSVEElekAVVVKIadrqwrysrfpevplfgraa 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1633 -QQMFDELRTWLDDKQSQQAKNCPISAKLERLHsqlqenEEFQKSLNQHSgsyevivaegeSLLLSVPPGEEKRTLQNQL 1711
Cdd:PRK04863 784 rEKRIEQLRAEREELAERYATLSFDVQKLQRLH------QAFSRFIGSHL-----------AVAFEADPEAELRQLNRRR 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1712 VELKNHWEELSKKTADRQSRLKDCMQKAQKYQWH--------VEDLVPWIEDCKAKMSELRVT-------------LDPV 1770
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQLDEAEEAkrfvqqhgnalaqLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1771 ------------QLESSLLRSKAMLSEVEKRRSLLEILNS---------AADILINSSEADEDgIRDEKAGINQNMDAIT 1829
Cdd:PRK04863 927 vsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSDLNEK-LRQRLEQAEQERTRAR 1005
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833258 1830 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLeifDALGSQACSNKnLEKLRAQQEVLQA 1895
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADSGA-EERARARRDELHA 1067
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
4221-4395 |
2.78e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4221 PSSPATPASGTKTSLQFSRcYDKPWLVNSKAGTPIRDSHSPDLQLPSPEVISSS--------GSKLKRPTPTFHSSRTSL 4292
Cdd:PHA03307 84 SRSTPTWSLSTLAPASPAR-EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEmlrpvgspGPPPAASPPAAGASPAAV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4293 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLLETQSAcSDT 4356
Cdd:PHA03307 163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGASSSD-SSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622833258 4357 SES--SAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 4395
Cdd:PHA03307 242 SESsgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1740-1840 |
2.90e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1740 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 1819
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833258 1820 GINQNMDAITEELQAKTGSLE 1840
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1373-1940 |
3.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1373 AENWKKIEEELN--------SRWERATEVTVARQRQLEESAGHLASFQAAESQLrpwmmEKElmmgvlgplsidpnmLNA 1444
Cdd:COG1196 212 AERYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEAELAEL-----EAE---------------LEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1445 QKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQE 1524
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1525 LLQDLSEKV--------RAVGQRLSGQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDE 1596
Cdd:COG1196 352 ELEEAEAELaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1597 LKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKS 1676
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1677 LNQHSGSYEVIVAEGESLLLSVPPGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQ 1740
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1741 KYQWHVEDLVpwiedckakMSELRVTLDPVQLESSLLRSKAMLSEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAG 1820
Cdd:COG1196 587 ALAAALARGA---------IGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1821 INQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQV 1900
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622833258 1901 DYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQR 1940
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2690-3125 |
3.31e-03 |
|
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: 43.56 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2690 EKTESLIQQYEAiSLLNSERYARLERAQVLVNQfwETYEELSPWIEETRALIAQLPPPA-IDHEQLRQQQEEMRQLRESI 2768
Cdd:pfam05483 222 EKIQHLEEEYKK-EINDKEKQVSLLLIQITEKE--NKMKDLTFLLEESRDKANQLEEKTkLQDENLKELIEKKDHLTKEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2769 AEHKPHIDKLLKIGPQLKE----------LNPEEGEMVEEKYHKAENMYAQIKEEVRQRALALDEAVSQSAQITEFH-DK 2837
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNeDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2838 IEPMLETLENLSSRL----RMPPLIPAEVDKIRECISDNKSATVELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQ 2913
Cdd:pfam05483 379 LKIITMELQKKSSELeemtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2914 ---DKLDQMVFFWE--DIKARAEEREIKFLDVLELAEKFWYDMAALlttIKDTQDIVHDLESPGIDPSIIKQQVE----A 2984
Cdd:pfam05483 459 ltaIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQEDIINCKKQEErmlkQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2985 AETIKEETDGLHEELEFIR---ILGADLIfACGETEKPEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQ 3061
Cdd:pfam05483 536 IENLEEKEMNLRDELESVReefIQKGDEV-KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833258 3062 SmfdwlDNTVIKLCTMPPvGTDLNTVKDQLNEMkEFKVEVYQQQIEMEKLNHQGELMLKKATDE 3125
Cdd:pfam05483 615 Q-----ENKALKKKGSAE-NKQLNAYEIKVNKL-ELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
714-824 |
3.56e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.62 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 714 QKFLQDHREFESWLERSEKELENMHKGGsSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDTENSFKEgkepse 793
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE------ 73
|
90 100 110
....*....|....*....|....*....|.
gi 1622833258 794 ignLVKDKLKDATERYTALHSECTRLGFHLN 824
Cdd:smart00150 74 ---EIEERLEELNERWEELKELAEERRQKLE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-592 |
3.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 386 SEHAQDLSPQ-QNRQMLRLLNELQRSFqeILE--QTAAQVDALQGHLQQMEQ-EALVKTLQKQQNTChQQLEDLCSWVGQ 461
Cdd:COG4913 190 SEKALRLLHKtQSFKPIGDLDDFVREY--MLEepDTFEAADALVEHFDDLERaHEALEDAREQIELL-EPIRELAERYAA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 462 AERALAGHQGRTTRQDLSALQKNQSDLKDLQDDIQnhatsfaavvkdiegfmeenqtklspHELTALREKLHQAKEQYEA 541
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRLELLEAELEELR--------------------------AELARLEAELERLEARLDA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622833258 542 LREQTRVAQKELEEAVTSALQQ-ETEKSKAAKELAENKKKIDALLDWVTSVG 592
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALG 372
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
4221-4395 |
3.67e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4221 PSSPATPASGTKTSLQFSRcydkpwlvnSKAGTPIRDSHSPdlqlPSPEViSSSGSKLKRPTPTFHSSRTSLAGDTSNSS 4300
Cdd:PHA03307 266 PTRIWEASGWNGPSSRPGP---------ASSSSSPRERSPS----PSPSS-PGSGPAPSSPRASSSSSSSRESSSSSTSS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 4301 SPASTGAKTnrADPKKSASRPGSRAGSRAGSRASSRRGSDASDfDLLETQSACSDTSESSAAGGQ---------GNSRRG 4371
Cdd:PHA03307 332 SSESSRGAA--VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS-RAPSSPAASAGRPTRRRARAAvagrarrrdATGRFP 408
|
170 180
....*....|....*....|....
gi 1622833258 4372 LNKPSKIPTmSKKTTTASPRTPGP 4395
Cdd:PHA03307 409 AGRPRPSPL-DAGAASGAFYARYP 431
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1546-2056 |
4.80e-03 |
|
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: 43.17 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1546 ISTQPEaVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGE--QYLKDELKKR----------LETVALPLQGLED 1613
Cdd:pfam05483 95 VSIEAE-LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEeiQENKDLIKENnatrhlcnllKETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1614 LAADRMNRLQAALASTQQFQQM---FDELRTwlddkqsqQAKNCPISA--KLERLHSQLQE-NEEFQKSLNQHSGSYEVi 1687
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMilaFEELRV--------QAENARLEMhfKLKEDHEKIQHlEEEYKKEINDKEKQVSL- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1688 vaegesLLLSVPPGEEK-RTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLvpwiedckaKMSELRVT 1766
Cdd:pfam05483 245 ------LLIQITEKENKmKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI---------KMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1767 LDPVQLESSL-LRSKAMLSEVEKRRSLLEILNSAA---DILINSSEAD----EDGIRDEKAGINQNMDA---ITEELQAK 1835
Cdd:pfam05483 310 STQKALEEDLqIATKTICQLTEEKEAQMEELNKAKaahSFVVTEFEATtcslEELLRTEQQRLEKNEDQlkiITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQ-------RLKEFQESFKNIEKKVEGAKHQLEIFDALgsQACSNKNLEKLRAQQEVLQALEPQVD------- 1901
Cdd:pfam05483 390 SSELEEMTKfknnkevELEELKKILAEDEKLLDEKKQFEKIAEEL--KGKEQELIFLLQAREKEIHDLEIQLTaiktsee 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1902 -YLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQRVNSGCVMMENKLEGIGQFHCRVREMFSQLADLDDEldgmg 1980
Cdd:pfam05483 468 hYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----- 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1981 avgrdTDSLQSQIEDVRL-FLNKIQVVKLDIEASEAECR----HMLEEEGTLDLL-----GLKRELEALNKQCGKLTERG 2050
Cdd:pfam05483 543 -----EMNLRDELESVREeFIQKGDEVKCKLDKSEENARsieyEVLKKEKQMKILenkcnNLKKQIENKNKNIEELHQEN 617
|
....*.
gi 1622833258 2051 KARQEQ 2056
Cdd:pfam05483 618 KALKKK 623
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1523-2059 |
5.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1523 QELLQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEET----SEIRSDLEQLDHEVKEAQTLCDELSVLIGEQylkDELK 1598
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELEELKEEI---EELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1599 KRLETVALPLQGLEdlaaDRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKSLN 1678
Cdd:PRK03918 245 KELESLEGSKRKLE----EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1679 QHSGSYEVIVAEGESLllsvppGEEKRTLQNQLVELKNHWEELsKKTADRQSRLKDCMQKAQKYQWHVEDLVPwiEDCKA 1758
Cdd:PRK03918 321 EEINGIEERIKELEEK------EERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTP--EKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1759 KMSELRVTLDPVQLESSLLRSK--AMLSEVEKRRSLLEILNSAADIL-INSSEADEdgirDEKAGInqnMDAITEELQAK 1835
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGKCpVCGRELTE----EHRKEL---LEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1836 TGSLEEMTQRLKEFQESFKNIEKKVEGAKH---QLEIFDALGS--QACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGL 1910
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESElikLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 1911 VEDApdgSDASQLLHQAEVTQQEFLEVKQRVNSgcvmMENKLEGIGqfhcrvremFSQLADLDDELDGMGAVGRDTDSLQ 1990
Cdd:PRK03918 545 KKEL---EKLEELKKKLAELEKKLDELEEELAE----LLKELEELG---------FESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833258 1991 SQIEDVRLFLNKIQVVKLDIEASEAEcrhmLEEEGTlDLLGLKRELEALNKQCGKLTERGKaRQEQLEL 2059
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEE----LAETEK-RLEELRKELEELEKKYSEEEYEEL-REEYLEL 671
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
395-583 |
6.30e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 395 QQNRQMLRLLNELQrsfqeileQTAAQVDALQGHLQQMEQEAlvktlqKQQNTCHQQLEDLCSWVGQAeralaghqgRTT 474
Cdd:COG3096 495 QTARELLRRYRSQQ--------ALAQRLQQLRAQLAELEQRL------RQQQNAERLLEEFCQRIGQQ---------LDA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 475 RQDLSALQknqSDLKDLQDDIQNHATSFAAVVKDIEgfMEENQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELE 554
Cdd:COG3096 552 AEELEELL---AELEAQLEELEEQAAEAVEQRSELR--QQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ 626
|
170 180 190
....*....|....*....|....*....|...
gi 1622833258 555 EaVTSALQQETEKSKAAK----ELAENKKKIDA 583
Cdd:COG3096 627 E-VTAAMQQLLEREREATverdELAARKQALES 658
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
3962-4013 |
6.83e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.91 E-value: 6.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833258 3962 ELKE-FANFDFD----VWRKKYMRWMNH-----KKSRVMDFFRRIDKDQDGKITRQEFIDGI 4013
Cdd:cd00051 1 ELREaFRLFDKDgdgtISADELKAALKSlgeglSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2361-2817 |
6.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2361 LSEKIDSLQARYSEIQDRccrkaalLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVfvkdfkQDVLHKQHADHLALNEE 2440
Cdd:PRK02224 277 LAEEVRDLRERLEELEEE-------RDDLLAEAGLDDADAEAVEARREELEDRDEEL------RDRLEECRVAAQAHNEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2441 IVNRKKNVDQA------IKNGQALLK---QTTGEEV-------LLIQEKLDGIKTRYTDITVTSSKA-------LRTLEQ 2497
Cdd:PRK02224 344 AESLREDADDLeeraeeLREEAAELEselEEAREAVedrreeiEELEEEIEELRERFGDAPVDLGNAedfleelREERDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2498 ARQLATKFQSTYEELTGWLREVEEELAASG----GQ----SPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLE 2569
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEAGKcpecGQpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2570 LVPWRARegldklVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADaELAWVAETKRKLMALGPIRLEQD-QTTAQ 2648
Cdd:PRK02224 504 LVEAEDR------IERLEERREDLEELIAERRETIEEKRERAEELRERAA-ELEAEAEEKREAAAEAEEEAEEArEEVAE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2649 LQVQKAFSIDIIRHKDSMDELFSHRSEifgtcgeeqktvLQEKTESLIQQYEAISLLNSERYARL----ERAQVLVNQFW 2724
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIAD------------AEDEIERLREKREALAELNDERRERLaekrERKRELEAEFD 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2725 ET-YEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNpEEGEMVEEKYHKA 2803
Cdd:PRK02224 645 EArIEEAREDKERAEEYLEQV------EEKLDELREERDDLQAEIGAVENELEELEELRERREALE-NRVEALEALYDEA 717
|
490
....*....|....*..
gi 1622833258 2804 E---NMYAQIKEEVRQR 2817
Cdd:PRK02224 718 EeleSMYGDLRAELRQR 734
|
|
| EFh_PEF_Group_I |
cd16180 |
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
3988-4050 |
7.19e-03 |
|
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.
Pssm-ID: 320055 [Multi-domain] Cd Length: 164 Bit Score: 40.20 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 3988 RVMDFFRRIDKDQDGKITRQEF-------------IDGI--LASKFPTT---KLEMT-------------AVADIFDRDG 4036
Cdd:cd16180 1 ELRRIFQAVDRDRSGRISAKELqralsngdwtpfsIETVrlMINMFDRDrsgTINFDefvglwkyiqdwrRLFRRFDRDR 80
|
90
....*....|....
gi 1622833258 4037 DGYIDYYEFVAALH 4050
Cdd:cd16180 81 SGSIDFNELQNALS 94
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2388-2918 |
8.11e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2388 QALSNAR-LFGEDEVEVLN---WLAEVEDKLSSV--FVKDFKQ-----DVLHKQHADHLALNEEI---VNRkknvDQAIK 2453
Cdd:COG3096 420 QALEKARaLCGLPDLTPENaedYLAAFRAKEQQAteEVLELEQklsvaDAARRQFEKAYELVCKIageVER----SQAWQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2454 NGQALLKQTTGEEVLLiqEKLDGIKTRYTDItvtsSKALRTLEQARQLATKFQ-------STYEELTGWLREVEEELA-A 2525
Cdd:COG3096 496 TARELLRRYRSQQALA--QRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCqrigqqlDAAEELEELLAELEAQLEeL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2526 SGGQSPTGEQIPQFQQRQKELKKEVMEHRlvldtvnevSRALLelvpWR-AREGLDKL-------VSDANE--------- 2588
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKELA---------ARAPA----WLaAQDALERLreqsgeaLADSQEvtaamqqll 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2589 ----QYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAELAWVAET-KRKLMA-----------------LGPIR---LEQD 2643
Cdd:COG3096 637 ererEATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERlGGVLLSeiyddvtledapyfsalYGPARhaiVVPD 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2644 QTTAQLQVQKAFSID-----IIRHKDSMDELFSHRSE-----------------------IFGTCGEEQK-TVLQEKTES 2694
Cdd:COG3096 717 LSAVKEQLAGLEDCPedlylIEGDPDSFDDSVFDAEEledavvvklsdrqwrysrfpevpLFGRAAREKRlEELRAERDE 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2695 LIQQY----------------------------------EAISLLNSERY---ARLERAQVLVNQFWETYEELSPWIEET 2737
Cdd:COG3096 797 LAEQYakasfdvqklqrlhqafsqfvgghlavafapdpeAELAALRQRRSeleRELAQHRAQEQQLRQQLDQLKEQLQLL 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2738 RALIAQL----PPPAIDH-EQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKElNPEEGEMVEEKYHKAENMYAQIK- 2811
Cdd:COG3096 877 NKLLPQAnllaDETLADRlEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQS-DPEQFEQLQADYLQAKEQQRRLKq 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2812 -----EEVRQR--ALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipaevDKIRECISDNKSATVELEKLQP 2884
Cdd:COG3096 956 qifalSEVVQRrpHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAR---------EQLRQAQAQYSQYNQVLASLKS 1026
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1622833258 2885 SFEA-------LKRRGEELiGRSQGADKDLAAKEIQDKLDQ 2918
Cdd:COG3096 1027 SRDAkqqtlqeLEQELEEL-GVQADAEAEERARIRRDELHE 1066
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
3988-4013 |
9.19e-03 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 36.61 E-value: 9.19e-03
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
3988-4013 |
9.60e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 36.39 E-value: 9.60e-03
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2091-2170 |
9.89e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 38.45 E-value: 9.89e-03
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833258 2091 VGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQLQE 2170
Cdd:pfam00435 29 YGKDLESVQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
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