|
Name |
Accession |
Description |
Interval |
E-value |
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
352-458 |
3.74e-71 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 234.55 E-value: 3.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 352 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 431
Cdd:cd21240 1 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1622833228 432 DAEDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
5324-5393 |
3.01e-39 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 141.82 E-value: 3.01e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5324 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 5393
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
5326-5394 |
2.24e-37 |
|
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: 136.19 E-value: 2.24e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 5326 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 5394
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1120-1197 |
1.05e-30 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 117.70 E-value: 1.05e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833228 1120 ISWNYLRKDLDLIQTWNLEKLRSSAPGECHQIMKNLQAHCEDFLQDSRDSVLFSVADRLRLEEEVEACKAHFQHLMKS 1197
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4429-4645 |
1.86e-30 |
|
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: 122.17 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4429 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 4508
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4509 RLETMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 4588
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 4589 REETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHAVSSKMEERKSKLEEAL 4645
Cdd:cd00176 158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4869-5081 |
1.07e-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: 119.86 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 5028
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 5029 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 5081
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4650-4864 |
1.23e-28 |
|
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: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4650 EFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 4729
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4730 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 4809
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4810 PVYDTTIRTGRALKEKtLLPEDTQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 4864
Cdd:cd00176 160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4209-4426 |
1.70e-24 |
|
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: 104.84 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4209 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 4288
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4289 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 4368
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833228 4369 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 4426
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
354-459 |
9.65e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.20 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYT-GIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTR 429
Cdd:pfam00307 1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKkLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 430 -LLDAEDVDvpSPDEKSVITYVSSIYDAFPK 459
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1019-1085 |
2.01e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 93.48 E-value: 2.01e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 1019 QLKPRSpdHLLKSTISVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCFLIP 1085
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3443-3656 |
2.65e-22 |
|
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: 98.67 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 3602
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 3603 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLEQAL 3656
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
358-453 |
3.32e-22 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 94.30 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR----ENLEQAFEVAERLGVTR-LLD 432
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVvLFE 80
|
90 100
....*....|....*....|.
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSI 453
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3988-4207 |
2.57e-19 |
|
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: 89.81 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3988 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 4067
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4068 KAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSrlrmpPLIPAEVDKIRECISDNKSATVELEK 4147
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4148 LQPSFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 4207
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
335-457 |
6.70e-19 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 95.01 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 335 LSWGLEEISDIYISGESGDMSAKEKLLLWTQKVTAGY-TGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN-- 411
Cdd:COG5069 105 LIWSLISRLTIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnk 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622833228 412 RENLEQAFEVAER-LGVTRLLDAEDV-DVPSPDEKSVITYVSSIYDAF 457
Cdd:COG5069 185 ALNNFQAFENANKvIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRF 232
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2788-3002 |
4.02e-17 |
|
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: 83.65 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2788 YQELLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 2867
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2868 ETVALPLQGLEDLAADRMNRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHS 2947
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 2948 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 3002
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4431-4532 |
2.05e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 75.06 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4431 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 4510
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 4511 ETMNQCWESVLQKTEEREQQLQ 4532
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1978-2206 |
1.19e-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: 73.25 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1978 ELQKFLQDHREFESWLERSEKELENMHkGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDtensfkEGKEP 2057
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2058 SEIgnlVKDKLKDATERYTALHSECTRLGFHLNMLLgQYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLA 2137
Cdd:cd00176 74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEA---ALASEDLGKDLESVEELLK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2138 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAI 2206
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3878-4090 |
1.19e-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: 73.25 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3878 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 3957
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3958 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEH 4037
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 4038 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYHKAENMYAQIKEEVRQRALALDEA 4090
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2194-2960 |
1.73e-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: 78.17 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2194 SLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 2273
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2274 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrff 2353
Cdd:TIGR02168 324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL--------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2354 qQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 2433
Cdd:TIGR02168 394 -QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2434 FQKWLKETEGSIpptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapDSQGKTGSILPSVGS 2513
Cdd:TIGR02168 473 AEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALL----------------KNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2514 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGilherqeSLQAILNRMEEVQKEANSVLQWLESKEE---VLKSMDAMS 2590
Cdd:TIGR02168 528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2591 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIEEE-----------LNSRW------ 2653
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2654 ERATEVTVARQRQLEESAGHLASFQAAESQLRPW--MMEKEL--MMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 2729
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAlaELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2730 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQR 2805
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2806 LSG----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSVLIgeqylkDELKKRLETVALPLQGLEDLA 2881
Cdd:TIGR02168 826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESEL------EALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2882 ADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESL 2960
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-----LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2977-3907 |
1.76e-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: 78.17 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2977 LVELKNHWEELskktaDRQSRlkdcmqKAQKYQwhvedlvpwiedckakmsELRVTLDPVQLESSLLRskaMLSEVEKRR 3056
Cdd:TIGR02168 195 LNELERQLKSL-----ERQAE------KAERYK------------------ELKAELRELELALLVLR---LEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3057 SLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAK 3130
Cdd:TIGR02168 243 ELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3131 HQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEvkqRVNSG 3210
Cdd:TIGR02168 323 AQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3211 CVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAVGRDtdsLQSQIEDVRLFLNKIQVVKLDIEASEAECRHMLEEE 3290
Cdd:TIGR02168 388 VAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3291 GTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLndattaAEEAEALQWVVGTEVEIINqqlad 3370
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELIS----- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3371 fkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW----------NTLNKKVAQRIAQLQEALL 3439
Cdd:TIGR02168 531 --------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3440 HCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiqeqkllqrlLDDRKATVDML------QAEG 3503
Cdd:TIGR02168 603 VAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT------------LDGDLVRPGGVitggsaKTNS 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3504 GRIAQSAELADREKitgQLKSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSE-PVGTQTA 3582
Cdd:TIGR02168 671 SILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3583 KIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDSLQARYSEIQDRCcrkaALLEQALSNARlf 3662
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELR-- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3663 gedevevlnwlAEVEDKLSSVFVKDFKQDVLHKQHADHLALNEEIVNRKKNV-DQAIKNGQALLKQTTGEEVLliQEKLD 3741
Cdd:TIGR02168 810 -----------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsEDIESLAAEIEELEELIEEL--ESELE 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3742 GIktrytditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAAsggqsptgeqipqFQQRQKELKKEVMEHRL 3821
Cdd:TIGR02168 877 AL-----------LNERASLEEALALL---RSELEELSEELRELESKRSE-------------LRRELEELREKLAQLEL 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3822 VLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYeqaadaelawVAETKRKLMAL 3901
Cdd:TIGR02168 930 RLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKEL 984
|
....*.
gi 1622833228 3902 GPIRLE 3907
Cdd:TIGR02168 985 GPVNLA 990
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4869-4969 |
3.77e-13 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 68.51 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLE 4969
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2563-2782 |
6.30e-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: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2563 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTyPNSQEAENW 2642
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIE-EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2643 KKIEEELNSRWERATEVTVARQRQLEESAGhLASFQAAESQLRPWMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 2722
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2723 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAI 2782
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
746-944 |
9.04e-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: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 746 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFR---TSYAETLGKLE 822
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdaEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 823 TQYCKLKETSSFRMRHLQ---SLHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSL 899
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622833228 900 QDTAELLSLENHPAKQtveaysAAVQSQLQWMKQLCLCVEQHVKE 944
Cdd:cd00176 166 NELAEELLEEGHPDAD------EEIEEKLEELNERWEELLELAEE 204
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4759-4861 |
2.86e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.81 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4759 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDTQKLDNF 4838
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833228 4839 LGEVRDKWDTVCGKSVERQHKLE 4861
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4431-4532 |
5.34e-12 |
|
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: 65.42 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4431 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 4510
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
|
90 100
....*....|....*....|..
gi 1622833228 4511 ETMNQCWESVLQKTEEREQQLQ 4532
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLE 104
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
5249-5311 |
1.15e-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: 60.25 E-value: 1.15e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 5249 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 5311
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
5249-5319 |
1.16e-10 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 62.50 E-value: 1.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622833228 5249 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 5319
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1591-1822 |
1.21e-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: 64.77 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1591 EKVKELLGWVStlarNTQGKATSSQTKES-TDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHklsekEKKQI 1669
Cdd:cd00176 7 RDADELEAWLS----EKEELLSSTDYGDDlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1670 SEQLNALNQAYHDLCDGSANQlqqlqsqlaHQTEQKTLQKQQNtcHQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQK 1749
Cdd:cd00176 78 QERLEELNQRWEELRELAEER---------RQRLEEALDLQQF--FRDADDLEQWLEEKEAALASED---LGKDLESVEE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 1750 NQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsPHELTALREKLHQAKEQYEALREQTRVAQKELEEA 1822
Cdd:cd00176 144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3659-3874 |
2.68e-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: 63.62 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3659 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 3738
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3739 KLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELaASGGQSPTGEQIPQFQQRQKELKKEVME 3818
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3819 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 3874
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3443-3544 |
1.28e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.50 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLE 3544
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4321-4423 |
1.42e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.50 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4321 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 4400
Cdd:smart00150 2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833228 4401 LTELKHLWENLGEKIAHRQHKLE 4423
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2896-2999 |
3.01e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 57.34 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2896 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 2975
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833228 2976 QLVELKNHWEELSKKTADRQSRLK 2999
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3988-4088 |
3.04e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 57.34 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3988 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 4067
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 4068 KAENMYAQIKEEVRQRALALD 4088
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
5247-5310 |
1.52e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 54.18 E-value: 1.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 5247 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 5310
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2896-3000 |
4.91e-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: 54.25 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2896 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 2975
Cdd:pfam00435 4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
|
90 100
....*....|....*....|....*
gi 1622833228 2976 QLVELKNHWEELSKKTADRQSRLKD 3000
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1620-2445 |
8.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1620 TDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEKKQISEQ--LNALNQAYHDLcdgsanqlqqlqsq 1697
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkeLYALANEISRL-------------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1698 lahQTEQKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEG 1777
Cdd:TIGR02168 301 ---EQQKQILRERLANLERQLEEL-----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1778 FMEENQTklsphELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKKidALLDWVTSV 1857
Cdd:TIGR02168 373 RLEELEE-----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1858 GSSGGQLLTNLPGMEQ---LSKASLEKGTLDTTDGYMGVNQAPEKLDKhCEKMKARHQELlsqqqhfilatQSAQAFLDQ 1934
Cdd:TIGR02168 446 EEELEELQEELERLEEaleELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGF-----------SEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1935 HGHNLtPEEQQMLQEKLgELKEQYSTSLaqsEAELKqvQTLQDELQKFLQDHREFESWLERSEkelenmhKGGSSPEALP 2014
Cdd:TIGR02168 514 NQSGL-SGILGVLSELI-SVDEGYEAAI---EAALG--GRLQAVVVENLNAAKKAIAFLKQNE-------LGRVTFLPLD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2015 SLLKR--QGSFSEDVISHKGDLRFVTIsgqkVLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSE---CTRLGFHL 2089
Cdd:TIGR02168 580 SIKGTeiQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGyriVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2090 N---MLLGQYHQFQNSADSLQAWMQTCEANVGKLLSDTVAsdpgvLQQQLATTKQLQEELAEHqvpVEKLQKVARDImei 2166
Cdd:TIGR02168 656 RpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE-----LEKALAELRKELEELEEE---LEQLRKELEEL--- 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2167 egepapdhkhvqettdsilshfqslSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEG-KQVVSLSSGVIQE 2245
Cdd:TIGR02168 725 -------------------------SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2246 ALATNMKLKQDIARQKSSLEATREMvtrfmetadsttaavlqgkLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLS 2325
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREA-------------------LDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2326 GKLQQFMENKSrmlasgnqpdqditrffQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLSQHQDRVQNLRKDFTE 2405
Cdd:TIGR02168 841 EDLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALALLRSELEE 898
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1622833228 2406 LQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSI 2445
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2560-2669 |
9.79e-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: 53.09 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2560 NRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 2639
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
|
90 100 110
....*....|....*....|....*....|
gi 1622833228 2640 ENWKKIeEELNSRWERATEVTVARQRQLEE 2669
Cdd:pfam00435 77 EIQERL-EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4869-4970 |
1.07e-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: 53.09 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLEQ 4970
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2095-2203 |
1.81e-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: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2095 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 2174
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
|
90 100
....*....|....*....|....*....
gi 1622833228 2175 KHVQETTDSILSHFQSLSYSLAERSSLLQ 2203
Cdd:pfam00435 76 EEIQERLEELNERWEQLLELAAERKQKLE 104
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3443-3545 |
9.18e-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: 50.39 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLED 3545
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4646-4752 |
1.80e-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: 49.62 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4646 NLATEFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLI 4725
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833228 4726 KNLLVSVQSRWEKVVQRSIERGRSLDD 4752
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2563-2668 |
2.47e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2563 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 2642
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833228 2643 KKIEEELNSRWERATEVTVARQRQLE 2668
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3471-4034 |
2.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3471 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLKSLESRWTELLSKAAARQKQLEDIL-VL 3549
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3550 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 3623
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3624 QGVLSEKIDSLQARYSEIQDRCCRKAALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHADHLAL 3703
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3704 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYTDIT---------VTSSKALRTLEQARQLATKFQst 3774
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3775 yeELTGWLREVE---EELAASGGQSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 3846
Cdd:COG1196 528 --VLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3847 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 3926
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3927 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 4006
Cdd:COG1196 685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1622833228 4007 IAQLPPPAIDHEQLRQQQEEMRQLRESI 4034
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5091-5215 |
3.41e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.87 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5091 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 5169
Cdd:smart00150 7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622833228 5170 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 5215
Cdd:smart00150 78 ----------------------RLEELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1614-1979 |
3.60e-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: 53.91 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1614 SQTKESTDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEkkqisEQLNALNQAYHDLCDGSANQLQQ 1693
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-----EELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1694 LQsqlAHQTEQKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRTTRQDLSALQKNqsdLKDLQDDIQNHATSFAAVVK 1773
Cdd:TIGR02168 735 LA---RLEAEVEQLEERIAQLSKELTEL-----EAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1774 DIEGFMEEnqtklspheLTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDW 1853
Cdd:TIGR02168 804 ALDELRAE---------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1854 VTSVGSSGGQLltnlpgMEQLSKASLEKGTLDTTDgymgvnqapEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLD 1933
Cdd:TIGR02168 875 LEALLNERASL------EEALALLRSELEELSEEL---------RELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622833228 1934 QHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDEL 1979
Cdd:TIGR02168 940 NLQERLS-EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1260-1988 |
4.52e-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: 53.52 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1260 QEDLQQLRSDLDAVSMKCDSFLHQ-SPSSSSVPTLRSELNLLVEKMDHVYGLSTVYLNKLKTVDVIVRSIQDAEllvkgy 1338
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL------ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1339 EIKLSQEEAVLADLSALEAHRSTLRHWFSDVKDKNSVFSV----LDEEIDKAKAVAEQMSRLTPERNLDLERYQEKGSQL 1414
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1415 QERWHRVIAQLEIRQSELESI--------QEVLGDYRACHGTLIKWIEETTAQQEMMKPGQAEDSRVLSEQLSQQTALFA 1486
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLedrrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1487 EIERNQTKLDQCQKFSQQYSTIVKDYELQLMTY----KAFVESQQKSPGKRRRmLSSSDAITQEF-----MDLRTRYTAL 1557
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGLSGILGV-LSELISVDEGYeaaieAALGGRLQAV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1558 VTLTTQHVKYISDALRR--------LEEEEKVVEEEKQEHVEKVKELLGWVSTLarntqgkatSSQTKESTDIEKAI--- 1626
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVA---------KDLVKFDPKLRKALsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1627 LEQQVLAEELTT-----KKEQVSEAIKTSQIFLAKHGHKLS-------------EKEKKQISEQLNALNQAYHDLcdgsa 1688
Cdd:TIGR02168 622 LGGVLVVDDLDNalelaKKLRPGYRIVTLDGDLVRPGGVITggsaktnssilerRREIEELEEKIEELEEKIAEL----- 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1689 nqlqqlqsqlahQTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGhqgrtTRQDLSALQKNQSDLKDLQDDIQNHATSF 1768
Cdd:TIGR02168 697 ------------EKALAELRKELEELEEELEQLRKELEELSRQISA-----LRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1769 AAVVKDIEGFMEENQTKLSPHE--LTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKK 1846
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEaeIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1847 IDALLDwvtSVGSSGGQLLTNLPGMEQL--SKASLEKGTLDTTDGYMGVNQAPEKLDKHCEKMKARHQELLSQQQHFILA 1924
Cdd:TIGR02168 840 LEDLEE---QIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 1925 TQSAQAFLDQHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHRE 1988
Cdd:TIGR02168 917 LEELREKLAQLELRLE-GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2097-2203 |
2.07e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2097 HQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDHKH 2176
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQ---LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE---EGHPDAEE 74
|
90 100
....*....|....*....|....*..
gi 1622833228 2177 VQETTDSILSHFQSLSYSLAERSSLLQ 2203
Cdd:smart00150 75 IEERLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
843-935 |
2.25e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 843 HKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYSA 922
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1622833228 923 AVQSQLQWMKQLC 935
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3979-4212 |
4.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3979 LERAQVLVNQFWETYEELSPWIEETRALIAQLPPPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 4058
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4059 GEMVEEKYHKAENMyaqikEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipAEVDKIRECISDN 4138
Cdd:PRK03918 265 EERIEELKKEIEEL-----EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------EEINGIEERIKEL 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4139 KSATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 4212
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1701-1849 |
4.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1701 QTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGrttrQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGfme 1780
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGG----DRLEQLEREIERLERELEERERRRARLEALLAALGL--- 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 1781 enQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSkaaKELAE---NKKKIDA 1849
Cdd:COG4913 374 --PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE---AEIASlerRKSNIPA 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2750-3127 |
5.27e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2750 TSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSGQSA----ISTQPEAVKQQLEE 2825
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2826 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRMNRLQAALASTQQFQQMFD 2903
Cdd:TIGR04523 307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2904 ELRTWLDDKQSQQAKNCPISAKLERLHSQLQE----NEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 2978
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2979 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSE 3051
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3052 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVE 3127
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4208-4314 |
6.14e-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: 45.39 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4208 ELAEKFWYDMAALLTTIKDTQDIVHDlESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFAcGETEKPEV 4287
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833228 4288 RKSIDEMNNAWENLNKTWKERLEKLED 4314
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3994-4089 |
1.02e-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: 44.62 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3994 EELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYHKAENMY 4073
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
|
90
....*....|....*.
gi 1622833228 4074 AQIKEEVRQRALALDE 4089
Cdd:pfam00435 90 EQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3003-3107 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3003 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRD 3082
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1622833228 3083 EKAGINQNMDAITEELQAKTGSLEE 3107
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2706-3263 |
2.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2706 NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTgpgdvslSTSQVQKELQSINQKWVELTDKlnsrstqIDQAIVKS 2785
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLE-------EHEERREELETLEAEIEDLRET-------IAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2786 TQYQELLQDLSEKVRAVGQRLSGQSAI----STQPEAVKQQLEE----TSEIRSDLEQL-----DHEvKEAQTLCDELSV 2852
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREEledrDEELRDRLEECrvaaqAHN-EEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2853 LIGEqylKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLHSQ 2932
Cdd:PRK02224 354 LEER---AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE---LREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2933 LQENEEFQKSLnqhsgsyEVIVAEGESLLLS---------------VPPGEEKR----TLQNQLVELKNHWEELSKKTaD 2993
Cdd:PRK02224 428 EAELEATLRTA-------RERVEEAEALLEAgkcpecgqpvegsphVETIEEDRerveELEAELEDLEEEVEEVEERL-E 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2994 RQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAmlseVEKRrslleilNSAADILINSS 3073
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA----EEKR-------EAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3074 EAdedgiRDEKAGINQNMDAITEELQaktgSLEemtqRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQacsnkNLEKLR 3153
Cdd:PRK02224 569 EA-----REEVAELNSKLAELKERIE----SLE----RIRTLLAAIADAEDEIERLREKREALAELNDE-----RRERLA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3154 AQQEVLQALEPQVDYLRnftqglVEDA-PDGSDASQLLHQAEVTQQEFLEVKQRVNSGCVMMENKLEgigqfhcRVREMF 3232
Cdd:PRK02224 631 EKRERKRELEAEFDEAR------IEEArEDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------ELEELR 697
|
570 580 590
....*....|....*....|....*....|.
gi 1622833228 3233 SQLADLDDELDGMGAVGRDTDSLQSQIEDVR 3263
Cdd:PRK02224 698 ERREALENRVEALEALYDEAEELESMYGDLR 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1745-2043 |
2.57e-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: 47.07 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1745 SALQKNQSDLKDLQDDIQNHATSFAAvvkdiegfmEENQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAvt 1824
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1825 salqqETEKSKAAKELAENKKKIDALLDWVtsvgssggQLLTNLPGMEQLSKASlekGTLDTTDGYMGVNQAPEKLDKHC 1904
Cdd:COG4942 89 -----EKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1905 EKMKARHQELLSQQQHFILATQSAQAFLDqhghnltpeEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQ 1984
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLA---------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 1985 DHREFESWLERSEKELENMHKGGSSPEA-----LP---SLLKRQGSFSEDVISHKGdlrfVTISGQK 2043
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALkgklpWPvsgRVVRRFGERDGGGGRNKG----IDIAAPP 286
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
3952-4212 |
3.62e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3952 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpppaidhEQLR 4021
Cdd:COG0497 116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4022 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYHKAENmYAQIKEEVRQRALALDE------ 4089
Cdd:COG0497 179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4090 -----AVSQSAQITEFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 4154
Cdd:COG0497 244 dllgqALRALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 4155 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 4212
Cdd:COG0497 311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2654-3161 |
8.51e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2654 ERATEVTVARQRQLEESAGHLASFQAAESQLRPwmMEKELmmgvlgplsidpnmlnAQKQQVQFMLKEFEAR-------- 2725
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LEQRL----------------RQQQRAERLLAEFCKRlgknldde 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2726 ------RQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQ-------SINQKWVELTDKLNSRSTQIDQAIVKSTQYQELL 2792
Cdd:PRK04863 554 deleqlQEELEARLESLSESVSEARERRMALRQQLEQLQariqrlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYM 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2793 QDLSEKVRAVGQRLSGqsaISTQPEAVKQQLEETSEIR-SDLEQLdhevkeaQTLCDELS-VLIGEQY----LKDE---- 2862
Cdd:PRK04863 634 QQLLERERELTVERDE---LAARKQALDEEIERLSQPGgSEDPRL-------NALAERFGgVLLSEIYddvsLEDApyfs 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2863 ----------LKKRLETVALPLQGLEDLAAD-----------RMNRLQAAL---ASTQQF-------------------- 2898
Cdd:PRK04863 704 alygparhaiVVPDLSDAAEQLAGLEDCPEDlyliegdpdsfDDSVFSVEElekAVVVKIadrqwrysrfpevplfgraa 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2899 -QQMFDELRTWLDDKQSQQAKNCPISAKLERLHsqlqenEEFQKSLNQHSgsyevivaegeSLLLSVPPGEEKRTLQNQL 2977
Cdd:PRK04863 784 rEKRIEQLRAEREELAERYATLSFDVQKLQRLH------QAFSRFIGSHL-----------AVAFEADPEAELRQLNRRR 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2978 VELKNHWEELSKKTADRQSRLKDCMQKAQKYQWH--------VEDLVPWIEDCKAKMSELRVT-------------LDPV 3036
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQLDEAEEAkrfvqqhgnalaqLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3037 ------------QLESSLLRSKAMLSEVEKRRSLLEILNS---------AADILINSSEADEDgIRDEKAGINQNMDAIT 3095
Cdd:PRK04863 927 vsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSDLNEK-LRQRLEQAEQERTRAR 1005
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3096 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLeifDALGSQACSNKnLEKLRAQQEVLQA 3161
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADSGA-EERARARRDELHA 1067
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1715-1820 |
1.10e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1715 HQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENqtklsPHELTAL 1794
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833228 1795 REKLHQAKEQYEALREQTRVAQKELE 1820
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2639-3206 |
1.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2639 AENWKKIEEELN--------SRWERATEVTVARQRQLEESAGHLASFQAAESQLrpwmmEKElmmgvlgplsidpnmLNA 2710
Cdd:COG1196 212 AERYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEAELAEL-----EAE---------------LEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2711 QKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQE 2790
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2791 LLQDLSEKV--------RAVGQRLSGQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDE 2862
Cdd:COG1196 352 ELEEAEAELaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2863 LKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKS 2942
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2943 LNQHSGSYEVIVAEGESLLLSVPPGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQ 3006
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3007 KYQWHVEDLVpwiedckakMSELRVTLDPVQLESSLLRSKAMLSEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAG 3086
Cdd:COG1196 587 ALAAALARGA---------IGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3087 INQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQV 3166
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622833228 3167 DYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQR 3206
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1108-1511 |
1.84e-03 |
|
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: 45.11 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1108 LWHQlhvNTKSLISWNYLRKDLD--LIQTWNLEKLRSSAPGECHQIMKNLQAHcedfLQDSRDSVLFSVADRLRLEEEVE 1185
Cdd:pfam15921 403 LWDR---DTGNSITIDHLRRELDdrNMEVQRLEALLKAMKSECQGQMERQMAA----IQGKNESLEKVSSLTAQLESTKE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1186 ACKAHFQHLM-KSMENEDKEETVAKMYISelknirlrLEEYEqrvvKRIQSLASSRTDRDARQDsaLRIAEQEHTQEDLQ 1264
Cdd:pfam15921 476 MLRKVVEELTaKKMTLESSERTVSDLTAS--------LQEKE----RAIEATNAEITKLRSRVD--LKLQELQHLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1265 QLRSdldaVSMKCDSF-LHQSPSSSSVPTLRSE---LNLLVEKMDHVYGLSTVYLNKLKtvdvivRSIQDAELLVKGYEI 1340
Cdd:pfam15921 542 HLRN----VQTECEALkLQMAEKDKVIEILRQQienMTQLVGQHGRTAGAMQVEKAQLE------KEINDRRLELQEFKI 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1341 KLSQEEAVLADLSA----LEAHRSTLRHWFSD----VKDknsVFSVLDEEIDKAKAVAEQMSRLTPERNLDLERYQEKGS 1412
Cdd:pfam15921 612 LKDKKDAKIRELEArvsdLELEKVKLVNAGSErlraVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1413 QLQERWHRVIAQLEIRQSELESIQEVLGDYRACHGTLIKwIEETTAQQEMMKPGQ--AEDSRVlseQLSQQTALFAEIER 1490
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-VAMGMQKQITAKRGQidALQSKI---QFLEEAMTNANKEK 764
|
410 420
....*....|....*....|.
gi 1622833228 1491 NQTKlDQCQKFSQQYSTIVKD 1511
Cdd:pfam15921 765 HFLK-EEKNKLSQELSTVATE 784
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3006-3106 |
1.97e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3006 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 3085
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 3086 GINQNMDAITEELQAKTGSLE 3106
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1381-1505 |
3.39e-03 |
|
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: 42.43 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1381 EEIDKAKAVAEQMSRLTPERNLDLERYQEkgsQLQERWHRVIAQLEIRQSELESIQEVLGDYRACHgTLIKWIEETTAQQ 1460
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLE---ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAAL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622833228 1461 EMMKPGQAEDSrvLSEQLSQQTALFAEIERNQTKLDQCQKFSQQY 1505
Cdd:cd00176 130 ASEDLGKDLES--VEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
5476-5650 |
3.60e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5476 PSSPATPASGTKTSLQFSRcYDKPWLVNSKAGTPIRDSHSPDLQLPSPEVISSS--------GSKLKRPTPTFHSSRTSL 5547
Cdd:PHA03307 84 SRSTPTWSLSTLAPASPAR-EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEmlrpvgspGPPPAASPPAAGASPAAV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5548 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLLETQSAcSDT 5611
Cdd:PHA03307 163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGASSSD-SSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622833228 5612 SES--SAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 5650
Cdd:PHA03307 242 SESsgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1634-2265 |
6.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1634 EELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEKK--QISEQLNALNQAYHDLcdgsanqlqqlqsqLAHQTEQKTLQKQQ 1711
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSElpELREELEKLEKEVKEL--------------EELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1712 NTCHQQLEDLCSWVGQAERALAGhqgrtTRQDLSALQKNQSDLKDLQDDIQNHATsfaavvkdIEGFMEEnqtklsphel 1791
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKELKELKEKAEEYIK--------LSEFYEE---------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1792 taLREKLHQAKEQYEALREQTRVAQKELEEAVtsalQQETEKSKAAKELAENKKKIDALLDWVTSVgSSGGQLLTNlpgM 1871
Cdd:PRK03918 305 --YLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEE---L 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1872 EQLSKASLEKGTLDTTDGYMGVNQAPEKLDKHCEKMKARHQEL---LSQQQHFILATQSAQAFLDQHGHNLTPEEQqmlq 1948
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELkkeIKELKKAIEELKKAKGKCPVCGRELTEEHR---- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1949 eklGELKEQYSTSLAQSEAELKqvqTLQDELQKFLQDHREFESWLERsEKELENMHKggsSPEALPSLLKRQGSFSEDVI 2028
Cdd:PRK03918 451 ---KELLEEYTAELKRIEKELK---EIEEKERKLRKELRELEKVLKK-ESELIKLKE---LAEQLKELEEKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2029 SHKGDL------RFVTISGQkVLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSECTRLGFhlnmllgqyhqfqNS 2102
Cdd:PRK03918 521 EKKAEEyeklkeKLIKLKGE-IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF-------------ES 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2103 ADSLQAWMQTCEANVGKLLSdtVASDPGVLQQQLATTKQLQEELAEHQvpvEKLQKVARDIMEIEGEPAPDHKHVQETTd 2182
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAF---EELAETEKRLEELRKELEELEKKYSEEE- 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2183 silshFQSLSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNMKLKQDIARQKS 2262
Cdd:PRK03918 661 -----YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
...
gi 1622833228 2263 SLE 2265
Cdd:PRK03918 736 LLK 738
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
352-458 |
3.74e-71 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 234.55 E-value: 3.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 352 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 431
Cdd:cd21240 1 GDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1622833228 432 DAEDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
355-458 |
9.09e-64 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 213.02 E-value: 9.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 433
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKeFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
355-458 |
5.33e-60 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 202.52 E-value: 5.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 1622833228 435 DVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21239 81 DVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
354-458 |
1.21e-48 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 170.20 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
355-457 |
3.60e-44 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 157.19 E-value: 3.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLDA 433
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEqELGIAKLLDA 81
|
90 100
....*....|....*....|....
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
355-457 |
2.76e-42 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 151.78 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 433
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQkLGLTKLLDP 81
|
90 100
....*....|....*....|....
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
354-458 |
1.71e-40 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 146.69 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
355-460 |
3.12e-40 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 146.30 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 433
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERqLGITKLLDP 84
|
90 100
....*....|....*....|....*..
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAFPKV 460
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFYHYFSKM 111
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
5324-5393 |
3.01e-39 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 141.82 E-value: 3.01e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5324 DKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 5393
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
342-457 |
7.22e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 142.50 E-value: 7.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIYISGesgdMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21216 1 IQDISVEE----LSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622833228 422 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21216 77 AEKhLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
5326-5394 |
2.24e-37 |
|
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: 136.19 E-value: 2.24e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 5326 IEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 5394
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
354-458 |
5.64e-36 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 133.70 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*.
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
354-459 |
3.06e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 131.91 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLD 432
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEqELGISQLLD 82
|
90 100
....*....|....*....|....*..
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSIYDAFPK 459
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYFSK 109
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
351-460 |
1.63e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 127.48 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 351 SGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTR 429
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKeLGLTK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 430 LLDAEDVDVPSPDEKSVITYVSSIYDAFPKV 460
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKM 111
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
342-457 |
5.00e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 123.02 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIyisGESGdMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21291 1 IADI---NEEG-LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622833228 422 AER-LGVTRLLDAEDV-DVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21291 77 ASKeIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
354-451 |
8.09e-32 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 122.25 E-value: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLE 83
|
90
....*....|....*....
gi 1622833228 433 AEDVDVPSPDEKSVITYVS 451
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
358-458 |
2.62e-31 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 120.23 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVA-ERLGVTRLLDAED 435
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1622833228 436 VDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
355-460 |
3.86e-31 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 120.93 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 433
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLDP 96
|
90 100
....*....|....*....|....*..
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAFPKV 460
Cdd:cd21322 97 EDVNMEAPDEKSIITYVVSFYHYFSKM 123
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1120-1197 |
1.05e-30 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 117.70 E-value: 1.05e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833228 1120 ISWNYLRKDLDLIQTWNLEKLRSSAPGECHQIMKNLQAHCEDFLQDSRDSVLFSVADRLRLEEEVEACKAHFQHLMKS 1197
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4429-4645 |
1.86e-30 |
|
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: 122.17 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4429 LGQFQHALEELMSWLTHTEELLDAQRPISgDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAgDDASSLRS 4508
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4509 RLETMNQCWESVLQKTEEREQQLQSTLQQAQgFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKA 4588
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 4589 REETYNQLLDKGRlMLLSRDDSGSGSKTEQSVALLEQKWHAVSSKMEERKSKLEEAL 4645
Cdd:cd00176 158 HEPRLKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
360-457 |
2.67e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.45 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 360 LLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED-VD 437
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDmVA 85
|
90 100
....*....|....*....|
gi 1622833228 438 VPSPDEKSVITYVSSIYDAF 457
Cdd:cd21253 86 LKVPDKLSILTYVSQYYNYF 105
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
355-460 |
3.93e-30 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 117.12 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 433
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
|
90 100
....*....|....*....|....*..
gi 1622833228 434 EDVDVPSPDEKSVITYVSSIYDAFPKV 460
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4869-5081 |
1.07e-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: 119.86 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHmLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRV 5028
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 5029 DVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETAL 5081
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4650-4864 |
1.23e-28 |
|
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: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4650 EFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQkQDVVLIKNLL 4729
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4730 VSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWkKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQ 4809
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4810 PVYDTTIRTGRALKEKtLLPEDTQKLDNFLGEVRDKWDTVCGKSVERQHKLEEAL 4864
Cdd:cd00176 160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
355-457 |
2.94e-28 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 111.75 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80
|
90 100
....*....|....*....|....
gi 1622833228 435 DVDVPS-PDEKSVITYVSSIYDAF 457
Cdd:cd21198 81 DMVLLSvPDKLSVMTYLHQIRAHF 104
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
358-457 |
4.69e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.22 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED- 435
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEm 82
|
90 100
....*....|....*....|..
gi 1622833228 436 VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4756-4972 |
1.81e-26 |
|
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: 110.61 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4756 RAKQFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDTQKL 4835
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4836 DNFLGEVRDKWDTVCGKSVERQHKLEEALLFSgQFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKEL 4915
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833228 4916 GKRTGTVQVLKRSGRELIENSR-DDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQAL 4972
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
342-463 |
2.35e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 107.09 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21290 4 IQDISVE----ETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622833228 422 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAFPKVPEG 463
Cdd:cd21290 80 AEKyLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAFSGAQKA 123
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
355-457 |
4.65e-26 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 105.64 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21255 81 DmVLLPIPDKLIVMTYLCQLRAHF 104
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
342-457 |
1.72e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 104.81 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21289 1 IQDISVE----ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622833228 422 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21289 77 AEKyLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
355-457 |
2.48e-25 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 103.59 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPTTLTID 87
|
90 100
....*....|....*....|....
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21199 88 EmVSMERPDWQSVMSYVTAIYKHF 111
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
358-459 |
3.93e-25 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 103.08 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERV-QIQSNRENLEQAFEVAER-LGVTRLLDAE 434
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQhLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1622833228 435 DVDVPSPDEKSVITYVSSIYDAFPK 459
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
342-462 |
7.79e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 102.86 E-value: 7.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21287 1 IQDISVE----ETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622833228 422 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAFPKVPE 462
Cdd:cd21287 77 AEKyLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAFSGAQK 119
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
355-457 |
9.35e-25 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 101.65 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 433
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELAdIAPLLEV 80
|
90 100
....*....|....*....|....*.
gi 1622833228 434 EDVDV--PSPDEKSVITYVSSIYDAF 457
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLYRHL 106
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4209-4426 |
1.70e-24 |
|
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: 104.84 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4209 LAEKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVR 4288
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4289 KSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSMfDWLDNTVIKLCTMPPvGTDLNTVKDQLNEMKEFKVEVY 4368
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833228 4369 QQQIEMEKLNHQGELMLKKATDEtDRDIIREPLTELKHLWENLGEKIAHRQHKLEGAL 4426
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
358-458 |
1.88e-24 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 100.80 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED 435
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1622833228 436 VDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
356-458 |
7.69e-24 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 99.09 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 356 AKEKLLLWTQKVTAGYtGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 434
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQEsLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1622833228 435 DVDVPSPDEKSVITYVSSIYDAFP 458
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
342-457 |
2.39e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 98.61 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 342 ISDIYISgesgDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEV 421
Cdd:cd21288 1 IQDISVE----ETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622833228 422 AER-LGVTRLLDAED-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21288 77 AEKhLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
358-457 |
8.07e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 96.00 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDV 436
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1622833228 437 DVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
354-459 |
9.65e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.20 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYT-GIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTR 429
Cdd:pfam00307 1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKkLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 430 -LLDAEDVDvpSPDEKSVITYVSSIYDAFPK 459
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
360-457 |
1.10e-22 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 95.68 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 360 LLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED-VD 437
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETsLGIPALLDAEDmVT 84
|
90 100
....*....|....*....|
gi 1622833228 438 VPSPDEKSVITYVSSIYDAF 457
Cdd:cd21197 85 MHVPDRLSIITYVSQYYNHF 104
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1019-1085 |
2.01e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 93.48 E-value: 2.01e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 1019 QLKPRSpdHLLKSTISVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCFLIP 1085
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3443-3656 |
2.65e-22 |
|
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: 98.67 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIANQKPPSAEyKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEpISDFLSVTEKKLANSEPVGTQTaKIQQQIIRHKALEEDIENHA 3602
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 3603 TDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARYSEIQDRCCRKAALLEQAL 3656
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
358-453 |
3.32e-22 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 94.30 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 358 EKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR----ENLEQAFEVAERLGVTR-LLD 432
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVvLFE 80
|
90 100
....*....|....*....|.
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSI 453
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
355-457 |
4.67e-22 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 94.15 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80
|
90 100
....*....|....*....|....
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21254 81 DmVLLAVPDKLTVMTYLYQIRAHF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4321-4535 |
1.36e-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: 96.36 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4321 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 4400
Cdd:cd00176 4 QFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4401 LTELKHLWENLGEKIAHRQHKLEGALLALgQFQHALEELMSWLTHTEELLDAQrPISGDPKVIEVELAKHHVLKNDVLAH 4480
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4481 QATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTL 4535
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
356-459 |
2.08e-20 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 89.54 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 356 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 434
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPE 80
|
90 100
....*....|....*....|....*.
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAFPK 459
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHFSN 106
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
355-457 |
5.23e-20 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 88.55 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87
|
90 100
....*....|....*....|....
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21257 88 EmMYTDRPDWQSVMQYVAQIYKYF 111
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
355-457 |
1.04e-19 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 87.82 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 434
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKSTLDIN 93
|
90 100
....*....|....*....|....
gi 1622833228 435 D-VDVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21256 94 EmVRTERPDWQSVMTYVTAIYKYF 117
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
355-454 |
1.15e-19 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 87.35 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 433
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80
|
90 100
....*....|....*....|..
gi 1622833228 434 ED-VDVPSPDEKSVITYVSSIY 454
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFY 102
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
355-452 |
1.35e-19 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 86.91 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYtgiKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNR-ENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|
gi 1622833228 433 AEDVDVPSPDEKSVITYVSS 452
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
355-455 |
1.79e-19 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 86.94 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERL-GVTRLLDA 433
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1622833228 434 EDVDV--PSPDEKSVITYVSSIYD 455
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4974-5218 |
2.18e-19 |
|
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: 90.20 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4974 QAEVFRDTVHMLLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIK 5053
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5054 HWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELlawiQWAETTLIQRDQEPIPQNIDRVKALIAEHQTFMEE 5133
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE----QWLEEKEAALASEDLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5134 MTRKQPDVDRVTKtykrkniepTHAPFIEKSRSGGRkslsqptpppmpilsqsEAKNPRINQLSARWQQVWLLALERQRK 5213
Cdd:cd00176 155 LEAHEPRLKSLNE---------LAEELLEEGHPDAD-----------------EEIEEKLEELNERWEELLELAEERQKK 208
|
....*
gi 1622833228 5214 LNDAL 5218
Cdd:cd00176 209 LEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3988-4207 |
2.57e-19 |
|
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: 89.81 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3988 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 4067
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4068 KAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSrlrmpPLIPAEVDKIRECISDNKSATVELEK 4147
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4148 LQPSFEALKRRGEELIGRSQgadkDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVL 4207
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4537-4754 |
5.16e-19 |
|
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: 89.04 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4537 QAQGFHSEIEDFLLELTRMESQLSASKPtGGLPETAREQLDTHMELYSQLKAREETYNQLLDKG-RLMLLSRDDSgsgSK 4615
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGeQLIEEGHPDA---EE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4616 TEQSVALLEQKWHAVSSKMEERKSKLEEALNLATEFQnSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANE 4695
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 4696 VNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDAR 4754
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
335-457 |
6.70e-19 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 95.01 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 335 LSWGLEEISDIYISGESGDMSAKEKLLLWTQKVTAGY-TGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN-- 411
Cdd:COG5069 105 LIWSLISRLTIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnk 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622833228 412 RENLEQAFEVAER-LGVTRLLDAEDV-DVPSPDEKSVITYVSSIYDAF 457
Cdd:COG5069 185 ALNNFQAFENANKvIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRF 232
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
355-455 |
9.81e-19 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 84.71 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDA 433
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLAdCVPLVEV 80
|
90 100
....*....|....*....|....
gi 1622833228 434 EDVDV--PSPDEKSVITYVSSIYD 455
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYN 104
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
357-454 |
1.01e-18 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 85.14 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 357 KEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLG-VTRLLDAED 435
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1622833228 436 -VDVPSPDEKSVITYVSSIY 454
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
354-457 |
1.96e-18 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 83.84 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 354 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21251 4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKeFGISPIMT 83
|
90 100
....*....|....*....|....*.
gi 1622833228 433 AEDV-DVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21251 84 GKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
359-457 |
2.06e-18 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 83.94 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 359 KLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDV- 436
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEReFGIPPVTTGKEMa 87
|
90 100
....*....|....*....|.
gi 1622833228 437 DVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYELF 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3354-3547 |
3.23e-17 |
|
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: 83.65 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3354 QWVVGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQ 3433
Cdd:cd00176 25 STDYGDDLESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE--IQERLEELNQRWEELRELAEERRQR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3434 LQEALLHCGKFQDALEpLLSWLADTEELIANQKPPSAEYKvVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA 3513
Cdd:cd00176 102 LEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD 179
|
170 180 190
....*....|....*....|....*....|....
gi 1622833228 3514 DREKITGQLKSLESRWTELLSKAAARQKQLEDIL 3547
Cdd:cd00176 180 ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2788-3002 |
4.02e-17 |
|
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: 83.65 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2788 YQELLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLigEQYLKDELKKRL 2867
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2868 ETVALPLQGLEDLAADRMNRLQAALAStQQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHS 2947
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE-AALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 2948 GSYEVIVAEGESLLLSVPPGEEkRTLQNQLVELKNHWEELSKKTADRQSRLKDCM 3002
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
359-457 |
7.62e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.46 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 359 KLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDVD 437
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEReFGIPPVTTGKEMA 87
|
90 100
....*....|....*....|.
gi 1622833228 438 -VPSPDEKSVITYVSSIYDAF 457
Cdd:cd21250 88 sAEEPDKLSMVMYLSKFYELF 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3549-3765 |
9.63e-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: 79.41 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3549 LAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAkIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLS 3628
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3629 EKIDSLQARYSEIQDRCCRKAALLEQALSNARLFgEDEVEVLNWLAEVEDKLSSVFVKDFKQDVlHKQHADHLALNEEIV 3708
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 3709 NRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYTDITVTSSKALRTLEQAR 3765
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4431-4532 |
2.05e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 75.06 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4431 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 4510
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 4511 ETMNQCWESVLQKTEEREQQLQ 4532
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
355-457 |
2.41e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 75.08 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLDA 433
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAEnELGITPVVSA 82
|
90 100
....*....|....*....|....
gi 1622833228 434 EDVdVPSPDEKSVITYVSSIYDAF 457
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFHSAF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2896-3108 |
4.34e-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: 77.49 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2896 QQFQQMFDELRTWLDDKQSQQAKNCPISaKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 2975
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2976 QLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQwHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKR 3055
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 3056 RSLLEILNSAADILINSSEADEDGIRDEKA-GINQNMDAITEELQAKTGSLEEM 3108
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLeELNERWEELLELAEERQKKLEEA 212
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
359-451 |
1.20e-14 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 73.87 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 359 KLLL-WTQKVTAGYtGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN-------------------------- 411
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622833228 412 ---------RENLEQAFEVAERLG-VTRLLDAEDVDVPSPDEKSVITYVS 451
Cdd:cd21224 82 lssellaneKRNFKLVQQAVAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
357-455 |
2.06e-14 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 71.99 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 357 KEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSN---RENLEQAFEVAERLGV--TRLL 431
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGLpeLDLF 80
|
90 100
....*....|....*....|....
gi 1622833228 432 DAEDVdVPSPDEKSVITYVSSIYD 455
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1978-2206 |
1.19e-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: 73.25 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1978 ELQKFLQDHREFESWLERSEKELENMHkGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDtensfkEGKEP 2057
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE------EGHPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2058 SEIgnlVKDKLKDATERYTALHSECTRLGFHLNMLLgQYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLA 2137
Cdd:cd00176 74 AEE---IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEA---ALASEDLGKDLESVEELLK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2138 TTKQLQEELAEHQVPVEKLQKVARDImeIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAI 2206
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3878-4090 |
1.19e-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: 73.25 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3878 QQYEQAADAELAWVAETKRKLMALGPIRLEQdQTTAQLQVQKAFSIDIIRHKDSMDELfSHRSEIFGTCGEEQKTVLQEK 3957
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3958 TESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSpWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEH 4037
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 4038 KPHIDKLLKIGPQLKELNPEEGEM-VEEKYHKAENMYAQIKEEVRQRALALDEA 4090
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2194-2960 |
1.73e-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: 78.17 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2194 SLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNmklKQDIARQKSSLEATREMVTR 2273
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2274 FMETADSTtAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrff 2353
Cdd:TIGR02168 324 QLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL--------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2354 qQIQELNLEMEDQQENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT 2433
Cdd:TIGR02168 394 -QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2434 FQKWLKETEGSIpptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapDSQGKTGSILPSVGS 2513
Cdd:TIGR02168 473 AEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALL----------------KNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2514 SVGSVNGYHTCKDLTeiqcdmsdvnlkyekLGGilherqeSLQAILNRMEEVQKEANSVLQWLESKEE---VLKSMDAMS 2590
Cdd:TIGR02168 528 LISVDEGYEAAIEAA---------------LGG-------RLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2591 SPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIEEE-----------LNSRW------ 2653
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyrivtldgdlVRPGGvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2654 ERATEVTVARQRQLEESAGHLASFQAAESQLRPW--MMEKEL--MMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQH 2729
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAlaELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2730 EQLNEAAQGILTGPGDVSLST----SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQR 2805
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELeerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2806 LSG----QSAISTQPEAVKQQLEETSEirsDLEQLDHEVKEAQTLCDELSVLIgeqylkDELKKRLETVALPLQGLEDLA 2881
Cdd:TIGR02168 826 LESlerrIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELESEL------EALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2882 ADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpisAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESL 2960
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-----LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2977-3907 |
1.76e-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: 78.17 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2977 LVELKNHWEELskktaDRQSRlkdcmqKAQKYQwhvedlvpwiedckakmsELRVTLDPVQLESSLLRskaMLSEVEKRR 3056
Cdd:TIGR02168 195 LNELERQLKSL-----ERQAE------KAERYK------------------ELKAELRELELALLVLR---LEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3057 SLLEILNSAADIL------INSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAK 3130
Cdd:TIGR02168 243 ELQEELKEAEEELeeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3131 HQLEifdalgsqacsnKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEvkqRVNSG 3210
Cdd:TIGR02168 323 AQLE------------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3211 CVMMENKLEGIGQfhcRVREMFSQLADLDDELDGMGAVGRDtdsLQSQIEDVRLFLNKIQVVKLDIEASEAECRHMLEEE 3290
Cdd:TIGR02168 388 VAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3291 GTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYRKLKGLndattaAEEAEALQWVVGTEVEIINqqlad 3370
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELIS----- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3371 fkmfqkeqVDP-LQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARW----------NTLNKKVAQRIAQLQEALL 3439
Cdd:TIGR02168 531 --------VDEgYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3440 HCG-------KFQDALEPLLSWLADTEEL---IANQKPPSAEYKVVKaqiqeqkllqrlLDDRKATVDML------QAEG 3503
Cdd:TIGR02168 603 VAKdlvkfdpKLRKALSYLLGGVLVVDDLdnaLELAKKLRPGYRIVT------------LDGDLVRPGGVitggsaKTNS 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3504 GRIAQSAELADREKitgQLKSLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSE-PVGTQTA 3582
Cdd:TIGR02168 671 SILERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3583 KIQQQIIRHKALEEDIENHATDVHQAvkigqslssltsPAEQGVLSEKIDSLQARYSEIQDRCcrkaALLEQALSNARlf 3662
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEA------------EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELR-- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3663 gedevevlnwlAEVEDKLSSVFVKDFKQDVLHKQHADHLALNEEIVNRKKNV-DQAIKNGQALLKQTTGEEVLliQEKLD 3741
Cdd:TIGR02168 810 -----------AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsEDIESLAAEIEELEELIEEL--ESELE 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3742 GIktrytditvtsSKALRTLEQARQLAtkfQSTYEELTGWLREVEEELAAsggqsptgeqipqFQQRQKELKKEVMEHRL 3821
Cdd:TIGR02168 877 AL-----------LNERASLEEALALL---RSELEELSEELRELESKRSE-------------LRRELEELREKLAQLEL 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3822 VLDtvnevsrallelvpwRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYeqaadaelawVAETKRKLMAL 3901
Cdd:TIGR02168 930 RLE---------------GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR----------LKRLENKIKEL 984
|
....*.
gi 1622833228 3902 GPIRLE 3907
Cdd:TIGR02168 985 GPVNLA 990
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4869-4969 |
3.77e-13 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 68.51 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAeDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLE 4969
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2563-2782 |
6.30e-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: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2563 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTyPNSQEAENW 2642
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDL---ESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIE-EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2643 KKIEEELNSRWERATEVTVARQRQLEESAGhLASFQAAESQLRPWMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEF 2722
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2723 EARRQQHEQLNEAAQGILTGPGDvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAI 2782
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2095-2311 |
6.42e-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: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2095 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 2174
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEE---LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2175 KHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLEsLSQSIGEVEQNLEgKQVVSLSSGVIQEALATNMKLK 2254
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 2255 QDIARQKSSLEATREMVTRFMETADSTTAAVLQGKLAEVSQRFEQLCLQQQEKESSL 2311
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
746-944 |
9.04e-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: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 746 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQNFR---TSYAETLGKLE 822
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdaEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 823 TQYCKLKETSSFRMRHLQ---SLHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSL 899
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622833228 900 QDTAELLSLENHPAKQtveaysAAVQSQLQWMKQLCLCVEQHVKE 944
Cdd:cd00176 166 NELAEELLEEGHPDAD------EEIEEKLEELNERWEELLELAEE 204
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4144-4316 |
1.36e-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: 70.17 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4144 ELEKLQPSFEALKRRGEELIgrsqgADKDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEKFWyDMAALLTT 4223
Cdd:cd00176 48 ELAAHEERVEALNELGEQLI-----EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4224 IKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVRKSIDEMNNAWENLNK 4303
Cdd:cd00176 122 LEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
|
170
....*....|...
gi 1622833228 4304 TWKERLEKLEDAM 4316
Cdd:cd00176 201 LAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
842-1033 |
1.40e-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: 70.17 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 842 LHKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYS 921
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 922 AAVQSQLQWMKQLCLCVEQHVKENTAYFQFFSDARELESFLRNLQDSIKrkySCDHNTSLSRLEDLLQDsmAQDEKEQLI 1001
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKK--HKELEEELE 156
|
170 180 190
....*....|....*....|....*....|..
gi 1622833228 1002 QSKSSVASLVGRSKTIVQLKPRSPDHLLKSTI 1033
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4759-4861 |
2.86e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.81 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4759 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTllPEDTQKLDNF 4838
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833228 4839 LGEVRDKWDTVCGKSVERQHKLE 4861
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
355-460 |
4.22e-12 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 65.48 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQKVTAGytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLD 432
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|....*...
gi 1622833228 433 AEDVDVPSPDEKSVITYVSSiydaFPKV 460
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLSQ----FPKA 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4431-4532 |
5.34e-12 |
|
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: 65.42 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4431 QFQHALEELMSWLTHTEELLdAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRL 4510
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
|
90 100
....*....|....*....|..
gi 1622833228 4511 ETMNQCWESVLQKTEEREQQLQ 4532
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLE 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2423-2670 |
1.94e-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: 67.09 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2423 QLDEFRKLVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASKGTLVEEINckgtplenlimeitapdsqg 2502
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2503 KTGSILPSVGSSvgsvngyhtckDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQkEANSVLQWLESKEEV 2582
Cdd:cd00176 61 ELGEQLIEEGHP-----------DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2583 LKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTYPNSQEAENWKKIeEELNSRWERATEVTVA 2662
Cdd:cd00176 129 LASEDLGKDL---ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL-EELNERWEELLELAEE 204
|
....*...
gi 1622833228 2663 RQRQLEES 2670
Cdd:cd00176 205 RQKKLEEA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3220-4118 |
5.99e-11 |
|
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: 69.70 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3220 GIGQFHCRVREMFSQLADLDDELDgmgavgrdtdslqsQIEDVRLFLNKiQVVKLDIEASEAECRHMLEEEG-------- 3291
Cdd:TIGR02168 166 GISKYKERRKETERKLERTRENLD--------------RLEDILNELER-QLKSLERQAEKAERYKELKAELrelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3292 TLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFyrklkglndattaaeeaealqwvvgteveiinqQLADF 3371
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------------------------------RLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3372 KMfqKEQVDPLQMKLQQVNGLgqgliqsagkdcdVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALlhcGKFQDALEPL 3451
Cdd:TIGR02168 278 EL--EEEIEELQKELYALANE-------------ISRLEQQKQILRERLANLERQLEELEAQLEELE---SKLDELAEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3452 LSWLADTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDrkatvdmlQAEGGRIAQSAELADREKITGQLKSLESRwte 3531
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEE--------QLETLRSKVAQLELQIASLNNEIERLEAR--- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3532 lLSKAAARQKQLEdilvlakqfhetaepisdflsvTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKI 3611
Cdd:TIGR02168 409 -LERLEDRRERLQ----------------------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3612 GQslssltspAEQGVLSEKIDSLQARYSEIQDRCcrkaALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVfvkdfkQD 3691
Cdd:TIGR02168 466 LR--------EELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVL------SE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3692 VLHKQHADHLALNEEIVNRKKNV----DQAIKNGQALLKQTTGEEVLLIQekLDGIKtrYTDITVTSSKALRTLEQARQL 3767
Cdd:TIGR02168 528 LISVDEGYEAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRVTFLP--LDSIK--GTEIQGNDREILKNIEGFLGV 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3768 ATKFQSTYEELTGWL--------------------REVEEEL--------------AASGGQSPTG-------------- 3799
Cdd:TIGR02168 604 AKDLVKFDPKLRKALsyllggvlvvddldnalelaKKLRPGYrivtldgdlvrpggVITGGSAKTNssilerrreieele 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3800 EQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLelvpwRAREGLDKLVSDANEQYKLVSDTIGQ---RVDEIDAAIQR 3876
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLR-----KELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTE 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3877 SQQYEQAADAELAWVAETKRKLMAlgpiRLEQDQTTAQlQVQKAFSIDIIRHKDSMDELFSHRSEIFGTcgEEQKTVLQE 3956
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA----EIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANL--RERLESLER 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3957 KTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAE 4036
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL------EEALALLRSELEELSEELRE 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4037 HKPHIDKLLKigpQLKELNPEEGEMvEEKYHKAENMYAQIKEEVRQRA-LALDEAVSQSAQITEFHDKIEPMLETLENLS 4115
Cdd:TIGR02168 906 LESKRSELRR---ELEELREKLAQL-ELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 1622833228 4116 SRL 4118
Cdd:TIGR02168 982 KEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2752-3600 |
7.39e-11 |
|
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: 69.32 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2752 QVQKELQSINQKWVELTDKLNSRSTQID----QAiVKSTQYQELLQDLSEKVRAV-GQRLsgqsaistqpeavKQQLEET 2826
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKslerQA-EKAERYKELKAELRELELALlVLRL-------------EELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2827 SEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKD-ELKKRLETvalpLQGledlaadRMNRLQAALASTQQFQQMFDEL 2905
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEE----LQK-------ELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2906 RTWLDDKQSQqakncpISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPpgEEKRTLQNQLVELKNHWE 2985
Cdd:TIGR02168 311 LANLERQLEE------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--AELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2986 ELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSA 3065
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3066 ADILINSSEADEDGIRDEKAGINQnmdaiteeLQAKTGSLEEMTQRLKEFQESFKNIEKkvegAKHQLE-IFDALGSQAC 3144
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLK----NQSGLSgILGVLSELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3145 SNKNLEKlraqqEVLQALEPQVDYLrnftqgLVEDAPDGSDASQLLHQAEVTQQEFLEVK----QRVNSGCVMMENKLEG 3220
Cdd:TIGR02168 531 VDEGYEA-----AIEAALGGRLQAV------VVENLNAAKKAIAFLKQNELGRVTFLPLDsikgTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3221 IGQFHCRVREMFSQL-ADLDDELDGMGAVgrdtDSLQSQIEDVRLFLNKIQVVKLDIEASEAecRHML---EEEGTLDLL 3296
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLrKALSYLLGGVLVV----DDLDNALELAKKLRPGYRIVTLDGDLVRP--GGVItggSAKTNSSIL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3297 GLKRELEALNKQCGKLTER---GKARQEQLELTLGRVEDFYRKL-KGLNDATTAAEEAEALQWVVGTEVEIINQQLADFK 3372
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKiaeLEKALAELRKELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3373 MFQKEQVDPLQMKLQQVNGLGQGLIQSAGKdcdVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLL 3452
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3453 SWLADTEELIANQkppSAEYKVVKAQIQ----EQKLLQRLLDDRKATVDMLQAEGGRIAQSAELA--DREKITGQLKSLE 3526
Cdd:TIGR02168 831 RRIAATERRLEDL---EEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLrsELEELSEELRELE 907
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 3527 SRWTELLSKAAARQKQLEDI-LVLAK---QFHETAEPISDFLSVT-EKKLANSEPVGTQTAKIQQQIIRhkaLEEDIEN 3600
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLeLRLEGlevRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKR---LENKIKE 983
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
5249-5311 |
1.15e-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: 60.25 E-value: 1.15e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 5249 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALH 5311
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
5249-5319 |
1.16e-10 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 62.50 E-value: 1.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622833228 5249 RVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTklEMTAVADIFDRDGDGYIDYYEFVAALhpnKDAYRP 5319
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAV---RDYYTP 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1591-1822 |
1.21e-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: 64.77 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1591 EKVKELLGWVStlarNTQGKATSSQTKES-TDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHklsekEKKQI 1669
Cdd:cd00176 7 RDADELEAWLS----EKEELLSSTDYGDDlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1670 SEQLNALNQAYHDLCDGSANQlqqlqsqlaHQTEQKTLQKQQNtcHQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQK 1749
Cdd:cd00176 78 QERLEELNQRWEELRELAEER---------RQRLEEALDLQQF--FRDADDLEQWLEEKEAALASED---LGKDLESVEE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 1750 NQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQtklsPHELTALREKLHQAKEQYEALREQTRVAQKELEEA 1822
Cdd:cd00176 144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGH----PDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2349-3169 |
1.23e-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: 68.54 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2349 ITRFFQQIQELNLEMEDQQENLDTLEHLVTELSScgfALDLSQHQ----DRVQNLRKDFTELQKTV-----KEREKDASS 2419
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELER---QLKSLERQaekaERYKELKAELRELELALlvlrlEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2420 CQEQLDEFRKLVRTFQKWLKETEGSIpptETSMSAK-ELEKQIEHLKSLLDDWAS--------KGTLVEEINCKGTPLEN 2490
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKL---EELRLEVsELEEEIEELQKELYALANeisrleqqKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2491 LIMEITAPDSQ-GKTGSILPSVGSSVGSVNgyhtcKDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQKEA 2569
Cdd:TIGR02168 321 LEAQLEELESKlDELAEELAELEEKLEELK-----EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2570 NSVLQWLESKEEVLKSMDAMSSPTKTETVKAQAESNKAFLAELEQNspkIQKVKEALAGLLVTYPNSQEAenwkkiEEEL 2649
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE---LEELEEELEELQEELERLEEA------LEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2650 NSRWERATEVTVARQRQLEESAGHLASFQAAESQL-------RPWMMEKELMMGVLGPLS----IDP------------- 2705
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvKALLKNQSGLSGILGVLSelisVDEgyeaaieaalggr 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2706 ------NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQId 2779
Cdd:TIGR02168 547 lqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2780 qAIVKS-TQYQELLQDLSEKVRAV---GQRLSGQSAISTQPEAVKQQLEETseiRSDLEQLDHEVKEAQTLCDELSVLIg 2855
Cdd:TIGR02168 626 -LVVDDlDNALELAKKLRPGYRIVtldGDLVRPGGVITGGSAKTNSSILER---RREIEELEEKIEELEEKIAELEKAL- 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2856 eqylkDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQmfdELRTWLDDKQSQQAKNCPISAKLERLHSQLQE 2935
Cdd:TIGR02168 701 -----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---EVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2936 NEEFQKSLNQHSGSYEVIVAEGEslllsvppgEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDL 3015
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLK---------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3016 VPWIEDCKAKMSElrvtldpvqLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAIT 3095
Cdd:TIGR02168 844 EEQIEELSEDIES---------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 3096 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEgAKHQLEIFDALgsqACSNKNLEKLRAQQEVLQALEPQVDYL 3169
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLTLEEAE---ALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2647-3367 |
2.30e-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: 67.77 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2647 EELNSRWERATEVTVARQRQLEESAGHLASFQAAESQLRPWM----MEKELMMGVLGPLSIDPNMLNAQKQ-------QV 2715
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleEEIEELQKELYALANEISRLEQQKQilrerlaNL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2716 QFMLKEFEARRQQHEQLNEAAQGILTgpgdvslstsQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDL 2795
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2796 SEKVRAVGQRLSGQSAistqpeavkqqleETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKdELKKRLETVAlplQ 2875
Cdd:TIGR02168 385 RSKVAQLELQIASLNN-------------EIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---E 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2876 GLEDLAAdRMNRLQAALASTqqfQQMFDELRTWLDDKQSQQAKncpISAKLERLHSQLQENEEFQKS-----LNQHSGSY 2950
Cdd:TIGR02168 448 ELEELQE-ELERLEEALEEL---REELEEAEQALDAAERELAQ---LQARLDSLERLQENLEGFSEGvkallKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2951 EVIVAegeSLLLSVPPGEEK-------RTLQNQLVELKNHWEE----LSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWI 3019
Cdd:TIGR02168 521 ILGVL---SELISVDEGYEAaieaalgGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3020 EDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSAADI------LINSSEADEDGIRDEKAGI---NQ 3089
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRkALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPGGVITGGSAKTNSSIlerRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3090 NMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQAcsNKNLEKLRAQQE-VLQALEPQVDY 3168
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEqLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3169 LRNFTQGLVEDAPDGSDASQLLHQAEVTQQeflEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQL-ADLDDELDGMGA 3247
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQIEQ----LKEELKALREALDELRAELTLLnEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3248 VGRDTDSLQSQIEDVRlflNKIQVVKLDIEASEAECRHM--LEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLEL 3325
Cdd:TIGR02168 829 LERRIAATERRLEDLE---EQIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1622833228 3326 TLGRVEDFYRKLKGLNDATTAAEEAEAlqwvvGTEVEIINQQ 3367
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLE-----GLEVRIDNLQ 942
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3659-3874 |
2.68e-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: 63.62 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3659 ARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHAdHLALNEEIVNRKKNVDQAIKNGQALLKQTtGEEVLLIQE 3738
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKK-HEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3739 KLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTyEELTGWLREVEEELaASGGQSPTGEQIPQFQQRQKELKKEVME 3818
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3819 HRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAI 3874
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2687-2892 |
3.30e-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: 63.23 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2687 WMMEKELMMGVLGPLSiDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSlstSQVQKELQSINQKWVE 2766
Cdd:cd00176 15 WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA---EEIQERLEELNQRWEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2767 LTDKLNSRSTQIDQAIVKSTQYQE---LLQDLSEKVRAVGQRLSGQSaistqPEAVKQQLEETSEIRSDLEQLDHEVKEA 2843
Cdd:cd00176 91 LRELAEERRQRLEEALDLQQFFRDaddLEQWLEEKEAALASEDLGKD-----LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622833228 2844 QTLCDELsVLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRLQAAL 2892
Cdd:cd00176 166 NELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
357-451 |
3.65e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 60.09 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 357 KEKLLLWTQKVTAGytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 434
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKReFNIPMVLSPE 81
|
90
....*....|....*..
gi 1622833228 435 DVDVPSPDEKSVITYVS 451
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3443-3544 |
1.28e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.50 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIAnQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLE 3544
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4321-4423 |
1.42e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.50 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4321 QYQDTLQSMFDWLDNTvIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDetDRDIIREP 4400
Cdd:smart00150 2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833228 4401 LTELKHLWENLGEKIAHRQHKLE 4423
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4650-4751 |
2.27e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 57.72 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4650 EFQNSLQEFINWLTLAEQSLNiASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLIKNLL 4729
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 4730 VSVQSRWEKVVQRSIERGRSLD 4751
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3770-3982 |
2.90e-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: 60.54 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3770 KFQSTYEELTGWLREVEEELAaSGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLELVPWRAREgLDKLV 3849
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3850 SDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAElAWVAETKRKLMALGPIRLEQDqTTAQLQVQKAFSIDIIRHK 3929
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 3930 DSMDELFSHRSEIFGTCGEEQKTVLQEKTESLIQQYEAISLLNSERYARLERA 3982
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2896-2999 |
3.01e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 57.34 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2896 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPgeEKRTLQN 2975
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833228 2976 QLVELKNHWEELSKKTADRQSRLK 2999
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3988-4088 |
3.04e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 57.34 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3988 QFWETYEELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYH 4067
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 4068 KAENMYAQIKEEVRQRALALD 4088
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
5247-5310 |
1.52e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 54.18 E-value: 1.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 5247 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 5310
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
355-459 |
1.84e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 55.85 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 355 SAKEKLLLWTQ-KVTAgytgIKCTNFSSCWSDGKMFNALIHRYRPDLV-DME----RVQIQSNRENLEQAfevAERLGVT 428
Cdd:cd21314 11 TPKQRLLGWIQnKVPQ----LPITNFNRDWQDGKALGALVDNCAPGLCpDWEswdpNQPVQNAREAMQQA---DDWLGVP 83
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 429 RLLDAEDVDVPSPDEKSVITYVSSiydaFPK 459
Cdd:cd21314 84 QVIAPEEIVDPNVDEHSVMTYLSQ----FPK 110
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3004-3219 |
2.15e-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: 57.84 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3004 KAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDE 3083
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3084 KAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKnIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALE 3163
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3164 PQVDYLRNFTQGLVEDAPDGSDAsqllhQAEVTQQEFLEVKQRVNSGCVMMENKLE 3219
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADE-----EIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2208-2415 |
2.19e-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: 57.84 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2208 QSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGViQEALATNMKLKQDIARQKSSLEATREMVTRFMEtADSTTAAVLQ 2287
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2288 GKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLSgKLQQFMENKSRMLASGNQPD--QDITRFFQQIQELNLEMED 2365
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2366 QQENLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFTELQKTVKEREK 2415
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4539-4642 |
2.94e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.64 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4539 QGFHSEIEDFLLELTRMESQLSaSKPTGGLPETAREQLDTHMELYSQLKAREETYNQLLDKGRLMLlsRDDSGSGSKTEQ 4618
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEE 77
|
90 100
....*....|....*....|....
gi 1622833228 4619 SVALLEQKWHAVSSKMEERKSKLE 4642
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
350-459 |
4.68e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 54.33 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 350 ESGDMSAKEKLLLWTQKvtaGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGV 427
Cdd:cd21313 3 DAKKQTPKQRLLGWIQN---KIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDwLGV 79
|
90 100 110
....*....|....*....|....*....|..
gi 1622833228 428 TRLLDAEDVDVPSPDEKSVITYVSSiydaFPK 459
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQ----FPK 107
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
352-459 |
4.73e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 54.40 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 352 GDMSAKEKLLLWTQ-KVTagytGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVT 428
Cdd:cd21315 13 KGPTPKQRLLGWIQsKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDwLDVP 88
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 429 RLLDAEDVDVPSPDEKSVITYVSsiydAFPK 459
Cdd:cd21315 89 QLIKPEEMVNPKVDELSMMTYLS----QFPN 115
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2896-3000 |
4.91e-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: 54.25 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2896 QQFQQMFDELRTWLDDKQsQQAKNCPISAKLERLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPGEEKrtLQN 2975
Cdd:pfam00435 4 QQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQE 80
|
90 100
....*....|....*....|....*
gi 1622833228 2976 QLVELKNHWEELSKKTADRQSRLKD 3000
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
5252-5310 |
5.94e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 54.80 E-value: 5.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 5252 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAAL 5310
Cdd:COG5126 37 TLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4978-5078 |
8.67e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.10 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4978 FRDTVHMLLEWLSEAEQTLRFRGaLPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWIT 5057
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 5058 IIRARFEEVLTWAKQHQQRLE 5078
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1620-2445 |
8.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1620 TDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEKKQISEQ--LNALNQAYHDLcdgsanqlqqlqsq 1697
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkeLYALANEISRL-------------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1698 lahQTEQKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEG 1777
Cdd:TIGR02168 301 ---EQQKQILRERLANLERQLEEL-----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1778 FMEENQTklsphELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKKidALLDWVTSV 1857
Cdd:TIGR02168 373 RLEELEE-----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1858 GSSGGQLLTNLPGMEQ---LSKASLEKGTLDTTDGYMGVNQAPEKLDKhCEKMKARHQELlsqqqhfilatQSAQAFLDQ 1934
Cdd:TIGR02168 446 EEELEELQEELERLEEaleELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGF-----------SEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1935 HGHNLtPEEQQMLQEKLgELKEQYSTSLaqsEAELKqvQTLQDELQKFLQDHREFESWLERSEkelenmhKGGSSPEALP 2014
Cdd:TIGR02168 514 NQSGL-SGILGVLSELI-SVDEGYEAAI---EAALG--GRLQAVVVENLNAAKKAIAFLKQNE-------LGRVTFLPLD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2015 SLLKR--QGSFSEDVISHKGDLRFVTIsgqkVLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSE---CTRLGFHL 2089
Cdd:TIGR02168 580 SIKGTeiQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGyriVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2090 N---MLLGQYHQFQNSADSLQAWMQTCEANVGKLLSDTVAsdpgvLQQQLATTKQLQEELAEHqvpVEKLQKVARDImei 2166
Cdd:TIGR02168 656 RpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE-----LEKALAELRKELEELEEE---LEQLRKELEEL--- 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2167 egepapdhkhvqettdsilshfqslSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEG-KQVVSLSSGVIQE 2245
Cdd:TIGR02168 725 -------------------------SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2246 ALATNMKLKQDIARQKSSLEATREMvtrfmetadsttaavlqgkLAEVSQRFEQLCLQQQEKESSLKKLLPQAEMFEHLS 2325
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREA-------------------LDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2326 GKLQQFMENKSrmlasgnqpdqditrffQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLSQHQDRVQNLRKDFTE 2405
Cdd:TIGR02168 841 EDLEEQIEELS-----------------EDIESLAAEIEELEELIEELESELEALLN-----ERASLEEALALLRSELEE 898
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1622833228 2406 LQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSI 2445
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2286-3139 |
8.91e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2286 LQGKLAEVSQRFEQLCLQQQEKES--SLKKLLPQAEMFEHLsGKLQQFMENKSRMLASGNQPDQDITRFFQQIQELNLEM 2363
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYELL-KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2364 EDQQENLDTLEHLVTELSScgfaldlsqhqdrvqnlrKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEG 2443
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGE------------------EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2444 SIPPTETSMsaKELEKQIEHLKSLLDDWAskgtlvEEINCKGTPLENLIMEITAPDsqgktgsilpsvgssvgsvngyht 2523
Cdd:TIGR02169 330 EIDKLLAEI--EELEREIEEERKRRDKLT------EEYAELKEELEDLRAELEEVD------------------------ 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2524 cKDLTEIQCDMSDVNLKYEKLGgilhERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSmdamssptKTETVKAQAE 2603
Cdd:TIGR02169 378 -KEFAETRDELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEA--------KINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2604 SNKAFLAELEQNSPKIQKVKEALAGLLvtypnSQEAENWKKIEEELNSRwERATEVTVARQRQLEESAGhlaSFQAAEsq 2683
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQEL-----YDLKEEYDRVEKELSKL-QRELAEAEAQARASEERVR---GGRAVE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2684 lrpwMMEKELMMGVLGPLS----IDP-----------NMLNA--------QKQQVQFmLKEFEARRQQHEQLNEAAQ--- 2737
Cdd:TIGR02169 514 ----EVLKASIQGVHGTVAqlgsVGEryataievaagNRLNNvvveddavAKEAIEL-LKRRKAGRATFLPLNKMRDerr 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2738 --GILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRA-VGQRLSGQSAIS- 2813
Cdd:TIGR02169 589 dlSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAmTGGSRAPRGGILf 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2814 --TQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLK-DELKKRLETVALPLQGLEDLAADRMNRLQA 2890
Cdd:TIGR02169 669 srSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKiGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2891 ALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLER--LHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVPPG- 2967
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEk 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2968 ----EEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ------ 3037
Cdd:TIGR02169 829 eyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieel 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3038 ------LESSLLRSKAMLSEVEKRRSLLEiLNSAADILINSSEADEDGIRDEKAGINQ--------NMDAIT--EELQAK 3101
Cdd:TIGR02169 909 eaqiekKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEeiralepvNMLAIQeyEEVLKR 987
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1622833228 3102 TGSLEEMTQRLKEFQESFKNIEKKVEGAKHQ--LEIFDAL 3139
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKKKREvfMEAFEAI 1027
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2560-2669 |
9.79e-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: 53.09 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2560 NRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVkEALAGLLVTYPNSQEA 2639
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL---ESVQALLKKHKALEAELAAHQDRVEAL-NELAEKLIDEGHYASE 76
|
90 100 110
....*....|....*....|....*....|
gi 1622833228 2640 ENWKKIeEELNSRWERATEVTVARQRQLEE 2669
Cdd:pfam00435 77 EIQERL-EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4869-4970 |
1.07e-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: 53.09 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4869 QFMDALQALVDWLYKVEPQLAEDQPVHgDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQ 4948
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1622833228 4949 ELSTRWDTVCKLSVSKQSRLEQ 4970
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4211-4313 |
1.44e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.72 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4211 EKFWYDMAALLTTIKDTQDIVHDLESPGiDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGEtEKPEVRKS 4290
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEER 78
|
90 100
....*....|....*....|...
gi 1622833228 4291 IDEMNNAWENLNKTWKERLEKLE 4313
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2095-2203 |
1.81e-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: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2095 QYHQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDH 2174
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYAS 75
|
90 100
....*....|....*....|....*....
gi 1622833228 2175 KHVQETTDSILSHFQSLSYSLAERSSLLQ 2203
Cdd:pfam00435 76 EEIQERLEELNERWEQLLELAAERKQKLE 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2140-2888 |
3.17e-07 |
|
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: 57.29 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2140 KQLQEELAEHQVpVEKLQKVARDI-MEIEGEPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLES 2218
Cdd:TIGR00618 166 KELLMNLFPLDQ-YTQLALMEFAKkKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2219 LSQSIGEVEQNLE-----GKQVVSLSSGVIQEALATNMKLKQDIARQKSSLEATREMVT--RFMETADSTTAAVLQGKLA 2291
Cdd:TIGR00618 245 LTQKREAQEEQLKkqqllKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTqiEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2292 EVSQRFEQLCLQQQEKES---SLKKLLPQAEMFEHLSGKLQQFMENKSRMLAsgnqpdqdITRFFQQIQELNLEMEDQQE 2368
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEqrrLLQTLHSQEIHIRDAHEVATSIREISCQQHT--------LTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2369 NLDTLEHLVTELSSCGFALDLSQHQDRVQNLRKDFT-ELQKTVKEREKDASSC--QEQLDEFRKLVRTFQKWlketegsi 2445
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqELQQRYAELCAAAITCtaQCEKLEKIHLQESAQSL-------- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2446 pptetsmsaKELEKQIEHLKSLLDDWASKGTLVEEINCKGTPLENLIMEITAPDSQGKTGSILPSVGSS--VGSVNGY-- 2521
Cdd:TIGR00618 469 ---------KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYaq 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2522 -HTCKDLTEIQCDmSDVNLKYEKLGGILHERQESL------QAILNRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPTK 2594
Cdd:TIGR00618 540 lETSEEDVYHQLT-SERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2595 TETVKAQAESNKAflAELEQNSPKIQKVKEALAGLLVTYPNSQEAENW---KKIEEELNSRWERATEVTVARQRQ----- 2666
Cdd:TIGR00618 619 RKLQPEQDLQDVR--LHLQQCSQELALKLTALHALQLTLTQERVREHAlsiRVLPKELLASRQLALQKMQSEKEQltywk 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2667 --LEESAGHLASFQAAESQLRPWMMEKELMMGVLGplsidpNMLNAQKQQVQFMLKEFEARR--QQHEQLNEAAQGILTG 2742
Cdd:TIGR00618 697 emLAQCQTLLRELETHIEEYDREFNEIENASSSLG------SDLAAREDALNQSLKELMHQArtVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2743 PGDVSLST--SQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRA-VGQRLSGQSAISTQpeaV 2819
Cdd:TIGR00618 771 TAALQTGAelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqFLSRLEEKSATLGE---I 847
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2820 KQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRL 2888
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
5252-5311 |
5.55e-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: 49.91 E-value: 5.55e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622833228 5252 DFFRRIDKDQDGKITRQEFIDGILASKFPTTKLemtavADIF---DRDGDGYIDYYEFVAALH 5311
Cdd:cd00052 3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL-----AQIWdlaDTDKDGKLDKEEFAIAMH 60
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3443-3545 |
9.18e-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: 50.39 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3443 KFQDALEPLLSWLADTEELIANQKPPSaEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAElADREKITGQL 3522
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833228 3523 KSLESRWTELLSKAAARQKQLED 3545
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4646-4752 |
1.80e-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: 49.62 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4646 NLATEFQNSLQEFINWLTLAEQSLNIASPPSLiLNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFlSQKQDVVLI 4725
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833228 4726 KNLLVSVQSRWEKVVQRSIERGRSLDD 4752
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4759-4862 |
1.96e-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: 49.62 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4759 QFHEAWKKLIDWLEDAESHLDSElEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKtlLPEDTQKLDNF 4838
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE--GHYASEEIQER 81
|
90 100
....*....|....*....|....
gi 1622833228 4839 LGEVRDKWDTVCGKSVERQHKLEE 4862
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2563-2668 |
2.47e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2563 EEVQKEANSVLQWLESKEEVLKSMDAMSSPtktETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLVTypNSQEAENW 2642
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL---ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833228 2643 KKIEEELNSRWERATEVTVARQRQLE 2668
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3471-4034 |
2.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3471 EYKVVKAQIQEQKLLQRLLDDRKATVDmLQAEGGRIAQSAelADREKITGQLKSLESRWTELLSKAAARQKQLEDIL-VL 3549
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAE-LEELEAELEELE--AELEELEAELAELEAELEELRLELEELELELEEAQaEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3550 AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSL------SSLTSPAE 3623
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3624 QGVLSEKIDSLQARYSEIQDRCCRKAALLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHKQHADHLAL 3703
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3704 NEEIVNRKKNVDQAIKNGQALLKQTTgEEVLLIQEKLDGIKTRYTDIT---------VTSSKALRTLEQARQLATKFQst 3774
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLeaeadyegfLEGVKAALLLAGLRGLAGAVA-- 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3775 yeELTGWLREVE---EELAASGGQSPTGEQIPQFQQRQKELKKEVME--HRLVLDTVNEVS---RALLELVPWRAREGLD 3846
Cdd:COG1196 528 --VLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAalaAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3847 KLVSDANEQYKLVSDTIGQRVDEIDAAIQRsQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDII 3926
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3927 RHKDSMDElfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRAL 4006
Cdd:COG1196 685 AERLAEEE-------------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1622833228 4007 IAQLPPPAIDHEQLRQQQEEMRQLRESI 4034
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2542-3133 |
2.88e-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: 54.35 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2542 EKLGGILHERQESLQAIL----NRMEEVQKEANSVLQWLESKEEVLKSmDAMSSPTKTETVKAQAES-NKAFLAELEQNS 2616
Cdd:pfam15921 245 DQLEALKSESQNKIELLLqqhqDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNqNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2617 PKIQKVKEALAGLLVTYPNsqeaenwkKIEEELNSRWERATEVTVAR--QRQLEESAGHL--------ASFQAAESQLRp 2686
Cdd:pfam15921 324 STVSQLRSELREAKRMYED--------KIEELEKQLVLANSELTEARteRDQFSQESGNLddqlqkllADLHKREKELS- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2687 wmMEKELM-------MG---VLGPLSIDPNMLNAQKQQVQFMLKEFEARRQ-QHEQLNEAAQGILTGPGDVSLSTSQvqk 2755
Cdd:pfam15921 395 --LEKEQNkrlwdrdTGnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQ--- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2756 eLQSINQKWVELTDKLNSRSTQIDQAivkSTQYQELLQDLSEKVRAVGqrlSGQSAISTQPEAVKQQLEETSEIRSDLEQ 2835
Cdd:pfam15921 470 -LESTKEMLRKVVEELTAKKMTLESS---ERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQELQHLKNEGDH 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2836 LDHevkeAQTLCDELSVLIGEQylkdelKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQ 2915
Cdd:pfam15921 543 LRN----VQTECEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2916 QAKNcpiSAKLERLHSQLQENEEFQKSLnqhsgsyeviVAEGESLLLSVPPGEEKRtlqNQLV-ELKNHWEELSKKTADR 2994
Cdd:pfam15921 613 KDKK---DAKIRELEARVSDLELEKVKL----------VNAGSERLRAVKDIKQER---DQLLnEVKTSRNELNSLSEDY 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2995 QSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLES--SLLRSKAMLSEVEKRRSLLEILNSAADIL--- 3069
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghAMKVAMGMQKQITAKRGQIDALQSKIQFLeea 756
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 3070 INSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQL 3133
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5091-5215 |
3.41e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.87 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5091 LEELLAWIQWAETTLiqrDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKR-KNIEPTHAPFIEKsrsggr 5169
Cdd:smart00150 7 ADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQlIEEGHPDAEEIEE------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622833228 5170 kslsqptpppmpilsqseaknpRINQLSARWQQVWLLALERQRKLN 5215
Cdd:smart00150 78 ----------------------RLEELNERWEELKELAEERRQKLE 101
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
353-455 |
3.56e-06 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 49.22 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 353 DMSAKEKLLLWTQK--VTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVD----MERVQIQSNRENLEQAFEVAERLG 426
Cdd:cd21218 8 YLPPEEILLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLG 87
|
90 100
....*....|....*....|....*....
gi 1622833228 427 VTRLLDAEDVdVpSPDEKSVITYVSSIYD 455
Cdd:cd21218 88 CKYFLTPEDI-V-SGNPRLNLAFVATLFN 114
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1614-1979 |
3.60e-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: 53.91 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1614 SQTKESTDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEkkqisEQLNALNQAYHDLCDGSANQLQQ 1693
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-----EELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1694 LQsqlAHQTEQKTLQKQQNTCHQQLEDLcswvgQAERALAGHQGRTTRQDLSALQKNqsdLKDLQDDIQNHATSFAAVVK 1773
Cdd:TIGR02168 735 LA---RLEAEVEQLEERIAQLSKELTEL-----EAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1774 DIEGFMEEnqtklspheLTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKKIDALLDW 1853
Cdd:TIGR02168 804 ALDELRAE---------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1854 VTSVGSSGGQLltnlpgMEQLSKASLEKGTLDTTDgymgvnqapEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLD 1933
Cdd:TIGR02168 875 LEALLNERASL------EEALALLRSELEELSEEL---------RELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622833228 1934 QHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDEL 1979
Cdd:TIGR02168 940 NLQERLS-EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1260-1988 |
4.52e-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: 53.52 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1260 QEDLQQLRSDLDAVSMKCDSFLHQ-SPSSSSVPTLRSELNLLVEKMDHVYGLSTVYLNKLKTVDVIVRSIQDAEllvkgy 1338
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL------ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1339 EIKLSQEEAVLADLSALEAHRSTLRHWFSDVKDKNSVFSV----LDEEIDKAKAVAEQMSRLTPERNLDLERYQEKGSQL 1414
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1415 QERWHRVIAQLEIRQSELESI--------QEVLGDYRACHGTLIKWIEETTAQQEMMKPGQAEDSRVLSEQLSQQTALFA 1486
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLedrrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1487 EIERNQTKLDQCQKFSQQYSTIVKDYELQLMTY----KAFVESQQKSPGKRRRmLSSSDAITQEF-----MDLRTRYTAL 1557
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGLSGILGV-LSELISVDEGYeaaieAALGGRLQAV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1558 VTLTTQHVKYISDALRR--------LEEEEKVVEEEKQEHVEKVKELLGWVSTLarntqgkatSSQTKESTDIEKAI--- 1626
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVA---------KDLVKFDPKLRKALsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1627 LEQQVLAEELTT-----KKEQVSEAIKTSQIFLAKHGHKLS-------------EKEKKQISEQLNALNQAYHDLcdgsa 1688
Cdd:TIGR02168 622 LGGVLVVDDLDNalelaKKLRPGYRIVTLDGDLVRPGGVITggsaktnssilerRREIEELEEKIEELEEKIAEL----- 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1689 nqlqqlqsqlahQTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGhqgrtTRQDLSALQKNQSDLKDLQDDIQNHATSF 1768
Cdd:TIGR02168 697 ------------EKALAELRKELEELEEELEQLRKELEELSRQISA-----LRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1769 AAVVKDIEGFMEENQTKLSPHE--LTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENKKK 1846
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEaeIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1847 IDALLDwvtSVGSSGGQLLTNLPGMEQL--SKASLEKGTLDTTDGYMGVNQAPEKLDKHCEKMKARHQELLSQQQHFILA 1924
Cdd:TIGR02168 840 LEDLEE---QIEELSEDIESLAAEIEELeeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 1925 TQSAQAFLDQHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHRE 1988
Cdd:TIGR02168 917 LEELREKLAQLELRLE-GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3552-3653 |
4.56e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.48 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3552 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQgVLSEKI 3631
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEERL 79
|
90 100
....*....|....*....|..
gi 1622833228 3632 DSLQARYSEIQDRCCRKAALLE 3653
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2548-3207 |
9.01e-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: 52.66 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2548 LHERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSMDAMSSPTKteTVKAQAESNKAFLAELEQNSPKI----QKVK 2623
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrarKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2624 EALAGLLVTYPNSQEAENWKKIEEELNSRW-ERATEVTVARQRQ-LEESAGHLASFQAAESQLRPWMMEKELMMGVLGPL 2701
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSsIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2702 SIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAqgiltgpgdvslstSQVQKELQSINqkwVELTDKLNSRSTQidqa 2781
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ--------------ATIDTRTSAFR---DLQGQLAHAKKQQ---- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2782 iVKSTQYQELLQDLSEKVRavgqrlsgQSAISTQPEAVK--QQLEETSEIRSDLEQLDHEVKEAQTLcdELSVLIGEQYL 2859
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTA--------QCEKLEKIHLQEsaQSLKEREQQLQTKEQIHLQETRKKAV--VLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2860 KDELKKRLETVALPLQGLEDLAADrMNRLQAALASTQQFQQMFDELRTWLDDKQSQqakncpisakLERLHSQLQENEEF 2939
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPL-TRRMQRGEQTYAQLETSEEDVYHQLTSERKQ----------RASLKEQMQEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2940 QKSLNQHSGSYEVIVAEGESLLLSVPP-GEEKRTLQNQLV-ELKNHWEELSKKTADRQSRLKD--CMQKAQKYQWHVEDL 3015
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDlTEKLSEAEDMLAcEQHALLRKLQPEQDLQDVRLHLqqCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3016 VPWIEDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSaADILINSSEADEDGIRDEKAGINQNMDAI 3094
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQ-CQTLLRELETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3095 TEELQAKTGSLEEMTQRLK-EFQESFKNIEKKVEGAKHQLEIFDALGSQacsnknLEKLRAQQEVLQ-ALEPQVDYLRNF 3172
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMhQARTVLKARTEAHFNNNEEVTAALQTGAE------LSHLAAEIQFFNrLREEDTHLLKTL 804
|
650 660 670
....*....|....*....|....*....|....*
gi 1622833228 3173 TQGLVEDAPDGSDAsqLLHQAEVTQQEFLEVKQRV 3207
Cdd:TIGR00618 805 EAEIGQEIPSDEDI--LNLQCETLVQEEEQFLSRL 837
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1817-2469 |
1.15e-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: 52.37 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1817 KELEEAVTSaLQQETEKSKAAKELAENKKKIDALLdWVTSVGSSGGQLLTNLpgmEQLSKASLEKGTLDTTdgymgVNQA 1896
Cdd:TIGR02168 196 NELERQLKS-LERQAEKAERYKELKAELRELELAL-LVLRLEELREELEELQ---EELKEAEEELEELTAE-----LQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1897 PEKLDKHCEKMKARHQELLSQQQHFiLATQSAQA-------FLDQHGHNL--TPEEQQMLQEKLGELKEQYSTSLAQSEA 1967
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKEL-YALANEISrleqqkqILRERLANLerQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1968 ELKQVQT----LQDELQKFLQDHREFESWLERSEKELENMHKGGSSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQK 2043
Cdd:TIGR02168 345 KLEELKEelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2044 VLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSECTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEANVGKLLS- 2122
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGf 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2123 -----------DTVASDPGVLQQQLATTKQ----LQEELAEH--QVPVEKLQKVARDI-----------------MEIEG 2168
Cdd:TIGR02168 505 segvkallknqSGLSGILGVLSELISVDEGyeaaIEAALGGRlqAVVVENLNAAKKAIaflkqnelgrvtflpldSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2169 EPAPDHKHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVqeslESLSQSIGEVEQNLEGKQVVSL------SSGV 2242
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV----DDLDNALELAKKLRPGYRIVTLdgdlvrPGGV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2243 I-QEALATNMKLkqdIARQKSSLEATREMvTRFMETADSTTAAV--LQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAE 2319
Cdd:TIGR02168 661 ItGGSAKTNSSI---LERRREIEELEEKI-EELEEKIAELEKALaeLRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2320 MFEHLSGKLQQFMENKSRMLAsgnQPDQDITRFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGFALD--LSQHQDRVQ 2397
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAELT 813
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 2398 NLRKDFTELQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMSakELEKQIEHLKSLLD 2469
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE--ELESELEALLNERA 883
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3948-4660 |
1.23e-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: 52.37 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3948 EEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEM 4027
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL------EQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4028 RQLRESIAEHKPHIDKLLK-----------IGPQLKELNPE---EGEMVEEKYHKAENM---YAQIKEEVRQRALALDEA 4090
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESkldelaeelaeLEEKLEELKEElesLEAELEELEAELEELesrLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4091 VSQ----SAQITEFHDKIEPMLETLENLSSRLR--MPPLIPAEVDKIRECISDNKSatvELEKLQPSFEALKRRGEELIG 4164
Cdd:TIGR02168 392 ELQiaslNNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4165 RSQGADKDL-AAKEIQDKLDQMVFFWEDIKARAEE--REIKFL---------------DVLELAEKFwydMAALLTTI-K 4225
Cdd:TIGR02168 469 ELEEAEQALdAAERELAQLQARLDSLERLQENLEGfsEGVKALlknqsglsgilgvlsELISVDEGY---EAAIEAALgG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4226 DTQDIVHDLESpgidpsiikQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPE-----VRKSIDEMNNAWEN 4300
Cdd:TIGR02168 546 RLQAVVVENLN---------AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgVAKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4301 LNKTWKERL---EKLEDAMQAAVQYQdtLQSMFDWLDNTVIKLCTMpPVGTDLNTVKDQLNEMKEFKvEVYQQQIEMEKL 4377
Cdd:TIGR02168 617 ALSYLLGGVlvvDDLDNALELAKKLR--PGYRIVTLDGDLVRPGGV-ITGGSAKTNSSILERRREIE-ELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4378 NHQGELMLKKATDETDRdiIREPLTELKHLWENLGEKIAHRQHKLEgallALGQFQHALEELMSWLTHTEELLDAQRpis 4457
Cdd:TIGR02168 693 IAELEKALAELRKELEE--LEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLEERIAQLSKELTELEAEI--- 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4458 gdpKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSaGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTLQQ 4537
Cdd:TIGR02168 764 ---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-REALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4538 AQGFHSEIEDFLLELTRMESQLSASkptGGLPETAREQLDTHMELYSQLKAREETYNQLLDKgrLMLLSRDDSGSGSKTE 4617
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEEL---EELIEELESELEALLNERASLEEALALLRSELEE--LSEELRELESKRSELR 914
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1622833228 4618 QSVALLEQKWHAVSSKMEERKSKLEEAL-NLATEFQNSLQEFIN 4660
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEA 958
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2070-2906 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2070 DATERYTALHSECTRLgfHLNMLLGQYHQFQNSADSLQawmQTCEANVGKLlsDTVASDPGVLQQQLATTK----QLQEE 2145
Cdd:TIGR02168 210 EKAERYKELKAELREL--ELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRlevsELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2146 LAEHQ----VPVEKLQKVARDIMEIEGEPAPDHKHVQETTDSILSHFQSLSySLAERSSLLQKAIAQSQSVQESLESLSQ 2221
Cdd:TIGR02168 283 IEELQkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-ELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2222 SIGEVEQNLEGK------QVVSLSSGVIQEALATNmKLKQDIARQKSSLEATREMVTRFMETADSTTAAVLQGKLAEVSQ 2295
Cdd:TIGR02168 362 ELEAELEELESRleeleeQLETLRSKVAQLELQIA-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2296 RFEQLCLQQQEKESSLkkllpqAEMFEHLSGKLQQFMENKSRMLASGNQpdqditrfFQQIQELNLEMEDQQENLDTLEH 2375
Cdd:TIGR02168 441 ELEELEEELEELQEEL------ERLEEALEELREELEEAEQALDAAERE--------LAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2376 LVTELSSCgfALDLSQHQDRVQNLRKdFTE-------------LQKTVKEREKDASSCQEQLDEFRKLVRTFQKWLKETE 2442
Cdd:TIGR02168 507 GVKALLKN--QSGLSGILGVLSELIS-VDEgyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2443 GSIPPTETSM---------SAKELEKQIEHLKSLLDDWASKGTLVEEINC-----KGTPLENLImeITapdsqgKTGSIL 2508
Cdd:TIGR02168 584 TEIQGNDREIlkniegflgVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNalelaKKLRPGYRI--VT------LDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2509 PSVGSSVGSVNGYHTckDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQKEANSVLQWLESKEEVLKSM-- 2586
Cdd:TIGR02168 656 RPGGVITGGSAKTNS--SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrk 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2587 DAMSSPTKTETVKAQAESNKAFLAELEQ----NSPKIQKVKEALAGLLVTYPNSQE-----AENWKKIEEELNSRWERAT 2657
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAeieeLEERLEEAEEELAEAEAEIEELEAqieqlKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2658 EVTVARQRQLEESAGHLASFQAAESQLRPWMMEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQ 2737
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2738 giltgpgdvsLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRlsgqsaisTQPE 2817
Cdd:TIGR02168 894 ----------SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--------TLEE 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2818 AvkqqLEETSEIRSDLEQLDHEVKEAQTLCDEL---SVLIGEQYlkDELKKRLETValpLQGLEDLAADRmNRLQAALA- 2893
Cdd:TIGR02168 956 A----EALENKIEDDEEEARRRLKRLENKIKELgpvNLAAIEEY--EELKERYDFL---TAQKEDLTEAK-ETLEEAIEe 1025
|
890
....*....|....*..
gi 1622833228 2894 ----STQQFQQMFDELR 2906
Cdd:TIGR02168 1026 idreARERFKDTFDQVN 1042
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3223-3438 |
1.37e-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: 49.75 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3223 QFHCRVREMFSQLADLDDELDGMGaVGRDTDSLQSQIEDVRLFLNKIQVVKLDIEASEAECRHMLEEeGTLDLLGLKREL 3302
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3303 EALNKQCGKLTERGKARQEQLELTLGRVEdFYRKLKGLNDATTAAEEAEALQwVVGTEVEIINQQLADFKMFQKEqVDPL 3382
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEE-LEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3383 QMKLQQVNGLGQGLIQSAGKDcDVQGLEHDMEEINARWNTLNKKVAQRIAQLQEAL 3438
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPD-ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3111-3324 |
1.87e-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: 49.37 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3111 RLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGLVEDAPDgsDASQLL 3190
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3191 HQAEVTQQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFSQLADLDDELDGMGA--VGRDTDSLQSQIEDVRLFLNK 3268
Cdd:cd00176 79 ERLEELNQRWEELRELAEE----RRQRLEEALDLQQFFRDADDLEQWLEEKEAALASedLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3269 IQVVKLDIEASEAECRHMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLE 3324
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2097-2203 |
2.07e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2097 HQFQNSADSLQAWMQTCEAnvgKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEKLQKVARDIMEiegEPAPDHKH 2176
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQ---LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE---EGHPDAEE 74
|
90 100
....*....|....*....|....*..
gi 1622833228 2177 VQETTDSILSHFQSLSYSLAERSSLLQ 2203
Cdd:smart00150 75 IEERLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
843-935 |
2.25e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 843 HKFVSRATAELIWLNEKEEEELAYDWSDNNSNISAKRNYFSELTMELEEKQDVFRSLQDTAELLSLENHPAKQTVEAYSA 922
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1622833228 923 AVQSQLQWMKQLC 935
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2973-3161 |
3.31e-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: 50.84 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2973 LQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ-----LESSLLRSK- 3046
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEealndLEARLSHSRi 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3047 ----AMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITE-------ELQAKTGSLEEMTQRLKEF 3115
Cdd:TIGR02169 794 peiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqiksiekEIENLNGKKEELEEELEEL 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622833228 3116 QESFKNIEKKVEGAKHQLEIFDALGSQACSNKN-----LEKLRAQQEVLQA 3161
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEeleaqIEKKRKRLSELKA 924
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2317-2559 |
4.06e-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: 48.21 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2317 QAEMFEHLSGKLQQFMENKSRMLASGNQPD--QDITRFFQQIQELNLEMEDQQENLDTLEHLVTELSSCGfALDLSQHQD 2394
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDdlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2395 RVQNLRKDFTELQKTVKEREKDASSCQEQLDEFRKlVRTFQKWLKETEGSIPPTETSMSAKELEKQIEHLKSLLDDWASK 2474
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2475 GTLVEEINCKGTPLENLimeitapdsqgktgsilpsvgssvgsvngyHTCKDLTEIQCDMSDVNLKYEKLGGILHERQES 2554
Cdd:cd00176 159 EPRLKSLNELAEELLEE------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
....*
gi 1622833228 2555 LQAIL 2559
Cdd:cd00176 209 LEEAL 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3979-4212 |
4.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3979 LERAQVLVNQFWETYEELSPWIEETRALIAQLPPPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEE 4058
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4059 GEMVEEKYHKAENMyaqikEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipAEVDKIRECISDN 4138
Cdd:PRK03918 265 EERIEELKKEIEEL-----EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------EEINGIEERIKEL 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4139 KSATVELEKLQPSFEALKRRGEELIGRSQgadkdlAAKEIQDKLDQMvffwEDIKARAEEREI-KFLDVLELAEK 4212
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEEL----ERLKKRLTGLTPeKLEKELEELEK 398
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4985-5078 |
4.91e-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: 45.39 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4985 LLEWLSEAEQTLRfRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDcITTIKHWITIIRARFE 5064
Cdd:pfam00435 13 LESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWE 90
|
90
....*....|....
gi 1622833228 5065 EVLTWAKQHQQRLE 5078
Cdd:pfam00435 91 QLLELAAERKQKLE 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1701-1849 |
4.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1701 QTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGrttrQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGfme 1780
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGG----DRLEQLEREIERLERELEERERRRARLEALLAALGL--- 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 1781 enQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSkaaKELAE---NKKKIDA 1849
Cdd:COG4913 374 --PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE---AEIASlerRKSNIPA 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2750-3127 |
5.27e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2750 TSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQDLSEKVRAVGQRLSGQSA----ISTQPEAVKQQLEE 2825
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqLKSEISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2826 --TSEIRSDLEQLDHEVKEAQTLCDELSVLIGEqyLKDElkkrletvalplqgLEDLAADRMNRLQAALASTQQFQQMFD 2903
Cdd:TIGR04523 307 dwNKELKSELKNQEKKLEEIQNQISQNNKIISQ--LNEQ--------------ISQLKKELTNSESENSEKQRELEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2904 ELRTWLDDKQSQQAKNCPISAKLERLHSQLQE----NEEFQKSLNQHSGSYEVIVAEGESLL-LSVPPGEEKRTLQNQLV 2978
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2979 ELKNHWEELSKKTADRQSRLKDCM-------QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSE 3051
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3052 VEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVE 3127
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4208-4314 |
6.14e-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: 45.39 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4208 ELAEKFWYDMAALLTTIKDTQDIVHDlESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFAcGETEKPEV 4287
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1622833228 4288 RKSIDEMNNAWENLNKTWKERLEKLED 4314
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
5261-5310 |
9.11e-05 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 43.07 E-value: 9.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622833228 5261 QDGKITRQEFIDGILASKFP-TTKLEMTAVADIFDRDGDGYIDYYEFVAAL 5310
Cdd:pfam13833 1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3745-4598 |
9.91e-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: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3745 TRYTDITVTSSKALRTLEQARQLATKFQstyeELTGWLREVEEELAASggqsptgeQIPQFQQRQKELKKEVMEHRLVLD 3824
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYK----ELKAELRELELALLVL--------RLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3825 TVNEVSRALLELVpwrarEGLDKLVSDANEQYklvsDTIGQRVDEIDAAIQRSQQYEQAADAELAwvaetkrklmalgpi 3904
Cdd:TIGR02168 257 ELTAELQELEEKL-----EELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLA--------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3905 RLEQDQTTAQLQVQKAFSiDIIRHKDSMDELfshrseifgtcgEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQV 3984
Cdd:TIGR02168 313 NLERQLEELEAQLEELES-KLDELAEELAEL------------EEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3985 LVNQFWETYEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAEH--KPHIDKLLKIGPQLKELNPEEgEMV 4062
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERL------EARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEEL-EEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4063 EEKYHKAENMYAQIKEEVRQRALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipaEVDKIRECISDNKSAT 4142
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK-------ALLKNQSGLSGILGVL 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4143 VELEKLQPSFE-----ALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFF----WEDIKARAEEREIK-----FLDVLE 4208
Cdd:TIGR02168 526 SELISVDEGYEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLpldsIKGTEIQGNDREILkniegFLGVAK 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4209 LAEKFWYDMAALLTTIKDTQDIVHDLESpgidpsiikqqveAAETIKEetdgLHEELEFIrILGADLIFACG----ETEK 4284
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGGVLVVDDLDN-------------ALELAKK----LRPGYRIV-TLDGDLVRPGGvitgGSAK 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4285 P-----EVRKSIDEmnnAWENLNKTwKERLEKLEDAMQAAVQYQDTLQSMFDWLDNTVIKLctmppvGTDLNTVKDQLnE 4359
Cdd:TIGR02168 668 TnssilERRREIEE---LEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL------SRQISALRKDL-A 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4360 MKEFKVEVYQQQIEMEKLNhQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEEL 4439
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4440 -MSWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLE---------SSAGDDASSLRSR 4509
Cdd:TIGR02168 816 nEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnerASLEEALALLRSE 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4510 LETMnqcwESVLQKTEEREQQLQSTLQQAQgfhSEIEDFLLELTRMESQLSaskptgGLPETAREQLDTHMELYSQLKAR 4589
Cdd:TIGR02168 896 LEEL----SEELRELESKRSELRRELEELR---EKLAQLELRLEGLEVRID------NLQERLSEEYSLTLEEAEALENK 962
|
....*....
gi 1622833228 4590 EETYNQLLD 4598
Cdd:TIGR02168 963 IEDDEEEAR 971
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3994-4089 |
1.02e-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: 44.62 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3994 EELSPWIEETRALIAQLPPPAiDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYHKAENMY 4073
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
|
90
....*....|....*.
gi 1622833228 4074 AQIKEEVRQRALALDE 4089
Cdd:pfam00435 90 EQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4321-4423 |
1.24e-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: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4321 QYQDTLQSMFDWLDNTVIKLcTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRdiIREP 4400
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
|
90 100
....*....|....*....|...
gi 1622833228 4401 LTELKHLWENLGEKIAHRQHKLE 4423
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLE 104
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3003-3107 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3003 QKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRD 3082
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1622833228 3083 EKAGINQNMDAITEELQAKTGSLEE 3107
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
3948-4198 |
1.45e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3948 EEQKTVLQEKTESLIQQYEAisllNSERYARLE------RAQVLVN--QFWETYEELSPWIEETRALIAQL--------P 4011
Cdd:PRK04778 118 EEDIEQILEELQELLESEEK----NREEVEQLKdlyrelRKSLLANrfSFGPALDELEKQLENLEEEFSQFveltesgdY 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4012 PPAidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGP-QLKELnpEEG--EMVEEKYH----KAENMYAQIKEEVRQ-- 4082
Cdd:PRK04778 194 VEA--REILDQLEEELAALEQIMEEIPELLKELQTELPdQLQEL--KAGyrELVEEGYHldhlDIEKEIQDLKEQIDEnl 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4083 ---RALALDEAvsqSAQITEFHDKIEPMLETLEN-LSSRLRMPPLIPAEVDKIRECISDNKSATVELEKLQPSFE----- 4153
Cdd:PRK04778 270 allEELDLDEA---EEKNEEIQERIDQLYDILEReVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTlnese 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622833228 4154 -----ALKRRGEELIGRSQGADKDLAAK-----EIQDKLDQMVFFWEDIKARAEE 4198
Cdd:PRK04778 347 lesvrQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEK 401
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
350-459 |
1.49e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 44.41 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 350 ESGDMSAKEKLLLWTQKvtaGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGV 427
Cdd:cd21312 7 EAKKQTPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGI 83
|
90 100 110
....*....|....*....|....*....|..
gi 1622833228 428 TRLLDAEDVDVPSPDEKSVITYVSSiydaFPK 459
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQ----FPK 111
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
746-840 |
1.63e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.86 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 746 LRFVYELLSWVEEMQMKLERAEWGNDLPSVELQLETQQHIHTSVEELGSSVKEARLYEGKMSQN---FRTSYAETLGKLE 822
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEghpDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1622833228 823 TQYCKLKETSSFRMRHLQ 840
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2706-3263 |
2.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2706 NMLNAQKQQVQFMLKEFEARRQQHEQLNEAAQGILTgpgdvslSTSQVQKELQSINQKWVELTDKlnsrstqIDQAIVKS 2785
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLE-------EHEERREELETLEAEIEDLRET-------IAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2786 TQYQELLQDLSEKVRAVGQRLSGQSAI----STQPEAVKQQLEE----TSEIRSDLEQL-----DHEvKEAQTLCDELSV 2852
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREEledrDEELRDRLEECrvaaqAHN-EEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2853 LIGEqylKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKncpISAKLERLHSQ 2932
Cdd:PRK02224 354 LEER---AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE---LREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2933 LQENEEFQKSLnqhsgsyEVIVAEGESLLLS---------------VPPGEEKR----TLQNQLVELKNHWEELSKKTaD 2993
Cdd:PRK02224 428 EAELEATLRTA-------RERVEEAEALLEAgkcpecgqpvegsphVETIEEDRerveELEAELEDLEEEVEEVEERL-E 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2994 RQSRLKDCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAmlseVEKRrslleilNSAADILINSS 3073
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA----EEKR-------EAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3074 EAdedgiRDEKAGINQNMDAITEELQaktgSLEemtqRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQacsnkNLEKLR 3153
Cdd:PRK02224 569 EA-----REEVAELNSKLAELKERIE----SLE----RIRTLLAAIADAEDEIERLREKREALAELNDE-----RRERLA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3154 AQQEVLQALEPQVDYLRnftqglVEDA-PDGSDASQLLHQAEVTQQEFLEVKQRVNSGCVMMENKLEgigqfhcRVREMF 3232
Cdd:PRK02224 631 EKRERKRELEAEFDEAR------IEEArEDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------ELEELR 697
|
570 580 590
....*....|....*....|....*....|.
gi 1622833228 3233 SQLADLDDELDGMGAVGRDTDSLQSQIEDVR 3263
Cdd:PRK02224 698 ERREALENRVEALEALYDEAEELESMYGDLR 728
|
|
| EFh_PEF_ALG-2_like |
cd16185 |
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
5253-5311 |
2.34e-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: 44.90 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5253 FFRRIDKDQDGKITRQEfIDGILASKFPTTKLEMTA-VADIFDRDGDGYIDYYEFvAALH 5311
Cdd:cd16185 5 WFRAVDRDRSGSIDVNE-LQKALAGGGLLFSLATAEkLIRMFDRDGNGTIDFEEF-AALH 62
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1745-2043 |
2.57e-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: 47.07 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1745 SALQKNQSDLKDLQDDIQNHATSFAAvvkdiegfmEENQTKLSPHELTALREKLHQAKEQYEALREQTRVAQKELEEAvt 1824
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1825 salqqETEKSKAAKELAENKKKIDALLDWVtsvgssggQLLTNLPGMEQLSKASlekGTLDTTDGYMGVNQAPEKLDKHC 1904
Cdd:COG4942 89 -----EKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1905 EKMKARHQELLSQQQHFILATQSAQAFLDqhghnltpeEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQ 1984
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLA---------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622833228 1985 DHREFESWLERSEKELENMHKGGSSPEA-----LP---SLLKRQGSFSEDVISHKGdlrfVTISGQK 2043
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALkgklpWPvsgRVVRRFGERDGGGGRNKG----IDIAAPP 286
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2253-2585 |
2.67e-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: 47.76 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2253 LKQDIARQKSSL-EATREM--VTRFMETAdSTTAAVLQGKLAEVSQRFEQLCLQQQEKEsslKKLLPQAEMFEHLSGKLQ 2329
Cdd:TIGR02169 693 LQSELRRIENRLdELSQELsdASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2330 QFMENKSRMLASGNQPDQDITRffQQIQELNLEMEDQQENLDTLEHLVTELSScgfalDLSQHQDRVQNLRKDFTELQKT 2409
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2410 VKEREKDASSCQEQLDEFRKLVRTFQKWLKETEGSIPPTETSMsaKELEKQIEHLKSLLDDWASK-GTLVEEINCKG--- 2485
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--GDLKKERDELEAQLRELERKiEELEAQIEKKRkrl 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2486 ----TPLENLIMEITAPDSQGKTGSILPSVGSSVGSVngYHTCKDLTEIQCDMSDVNLKYEKLGGILHERQESLQAILNR 2561
Cdd:TIGR02169 920 selkAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
330 340
....*....|....*....|....
gi 1622833228 2562 MEEvqkEANSVLQWLESKEEVLKS 2585
Cdd:TIGR02169 998 LEE---ERKAILERIEEYEKKKRE 1018
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
3952-4212 |
3.62e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3952 TVLQEKTESLIQ---QYEAISLLNSE-------RYARLERaqvLVNQFWETYEELspwieetRALIAQLpppaidhEQLR 4021
Cdd:COG0497 116 SQLRELGELLVDihgQHEHQSLLDPDaqrelldAFAGLEE---LLEEYREAYRAW-------RALKKEL-------EELR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4022 QQQEEMRQ----LRESIAEhkphidkllkigpqLKELNPEEGEMVE--EKYHKAENmYAQIKEEVRQRALALDE------ 4089
Cdd:COG0497 179 ADEAERAReldlLRFQLEE--------------LEAAALQPGEEEEleEERRRLSN-AEKLREALQEALEALSGgeggal 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4090 -----AVSQSAQITEFHDKIEPMLETLENLSsrlrmpplipAEVDKIRECISDNKSATV----ELEKLQpsfE------A 4154
Cdd:COG0497 244 dllgqALRALERLAEYDPSLAELAERLESAL----------IELEEAASELRRYLDSLEfdpeRLEEVE---ErlallrR 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 4155 LKRR-G---EELIGRsqgadkdlaAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEK 4212
Cdd:COG0497 311 LARKyGvtvEELLAY---------AEELRAELAELENSDERLEELEAELAEAEAELLEAAEK 363
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1628-2369 |
4.84e-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: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1628 EQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEKKQISEQLnaLNQAYHDLCDGSANQLQQLQSQLAHQTEQKTL 1707
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLC--TPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1708 QKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQTKLS 1787
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1788 phELTALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAkELAENKKKIDALLDWvtsvgssgGQLLTN 1867
Cdd:TIGR00618 322 --SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE-ISCQQHTLTQHIHTL--------QQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1868 LPGMEQLSKASLEK-----GTLDTTDgymgVNQAPEKLDKhcekMKARHQELLSQQQHFILATQSAQAFLDQHGHNLtpe 1942
Cdd:TIGR00618 391 LTQKLQSLCKELDIlqreqATIDTRT----SAFRDLQGQL----AHAKKQQELQQRYAELCAAAITCTAQCEKLEKI--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1943 EQQMLQEKLGELKEQystsLAQSEAELKQVQTLQDELQKFLQDHREFESWLERSEKE--------------------LEN 2002
Cdd:TIGR00618 460 HLQESAQSLKEREQQ----LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpnparqdidnpgpltrrmqrGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2003 MHKGGSSPEA-----LPSLLKRQGSFSEDVISHKGDLRFVTISGQKVldTENSFKEGKEPSEIGNLVKDKLKDATERYTA 2077
Cdd:TIGR00618 536 TYAQLETSEEdvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2078 LHSECTRLGFHLNMLLGQYHQfQNSADSLQAWMQTCEANVGKLLSDTV---ASDPGVLQQQLATTKQLQEELAEHQVP-- 2152
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLTLTQERVrehALSIRVLPKELLASRQLALQKMQSEKEql 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2153 ------VEKLQKVARDIMEIEGEPAPdhkHVQETTDSILSHFQSLSYSLAERSSLLQKAIAQSQSVQESLE--------- 2217
Cdd:TIGR00618 693 tywkemLAQCQTLLRELETHIEEYDR---EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTeahfnnnee 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2218 -----SLSQSIGEVEQNLEGKQvvSLSSGVIQEALATNMKLKQDIARQKSSLEATREMVTRFMETADST---------TA 2283
Cdd:TIGR00618 770 vtaalQTGAELSHLAAEIQFFN--RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRleeksatlgEI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2284 AVLQGKLAEVSQRFEQLCLQQQEKESSLKKLlpqaemfEHLSGKLQQFMENKSRMLASGNQPDQDITRFFQQIQELNLEM 2363
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDKL-------NGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRY 920
|
....*.
gi 1622833228 2364 EDQQEN 2369
Cdd:TIGR00618 921 ADSHVN 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3476-4406 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3476 KAQIQEQKLLQRLLDDRKATVDMLQAEggriaqsAELADREKITGQLKSLESRWTELLSKAAARQKQLEDILVLAKQFHE 3555
Cdd:TIGR02169 207 REKAERYQALLKEKREYEGYELLKEKE-------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3556 TAEPISDFLSVTekklansepVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQS-LSSLTSPAEQgvLSEKIDSL 3634
Cdd:TIGR02169 280 KIKDLGEEEQLR---------VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAeIDKLLAEIEE--LEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3635 QARYSEIQDRCCRKAALLEQALSNArlfGEDEVEvlnwLAEVEDKLSSVFVKdfkQDVLHKQHADHLALNEEIVNRKKNV 3714
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAEL---EEVDKE----FAETRDELKDYREK---LEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3715 DQAIKNGQALLKQttgeevllIQEKLDGIKTRYTDITVTSSKALRTLEQARQLATKFQSTYEELTGWLREVEEELAASgg 3794
Cdd:TIGR02169 419 SEELADLNAAIAG--------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3795 qsptGEQIPQFQQRQKELKKEVMEHRLVLDTVNEvsrallelvpwrAREGLDKLVSD---ANEQYKL-VSDTIGQRVDEI 3870
Cdd:TIGR02169 489 ----QRELAEAEAQARASEERVRGGRAVEEVLKA------------SIQGVHGTVAQlgsVGERYATaIEVAAGNRLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3871 ----DAAIQRSQQY---EQAADAELAWVAETKRKLMALGPIRLEQdqttaqlqvQKAFSIDIIRHKDSMDELFSHrseIF 3943
Cdd:TIGR02169 553 vvedDAVAKEAIELlkrRKAGRATFLPLNKMRDERRDLSILSEDG---------VIGFAVDLVEFDPKYEPAFKY---VF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3944 GTcgeeqkTVLQEKTES---LIQQYEAISLLNS--ER-------YARLERAQVLVNQFWETYEELSPWIEETRALIAQLp 4011
Cdd:TIGR02169 621 GD------TLVVEDIEAarrLMGKYRMVTLEGElfEKsgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4012 ppaidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKigpQLKELNPEEGEMVEEkyhkAENMYAQIKEEVRQRALALDEAV 4091
Cdd:TIGR02169 694 -----QSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKER----LEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4092 SQSAQITEFHDKIEPMLETLENLSSRLRMPPL--IPAEVDKIRECISDNKSATVELEKlqpsfeALKRRGEEligrsqga 4169
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIEQ------KLNRLTLE-------- 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4170 dKDLAAKEIQDKLDQMvffwEDIKARAEEREikflDVLELAEKFwydMAALLTTIKDTQDIVHDLESPGIDpsiikqqve 4249
Cdd:TIGR02169 828 -KEYLEKEIQELQEQR----IDLKEQIKSIE----KEIENLNGK---KEELEEELEELEAALRDLESRLGD--------- 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4250 aaetIKEETDGLHEELEfirilgadlifacgetekpEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQSM 4329
Cdd:TIGR02169 887 ----LKKERDELEAQLR-------------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4330 FDwldntviklctMPPVGTDLNTVKDQLNEMKE---------FKVEvyqQQIEmEKLNHQGELMLKKATDETDRDIIR-- 4398
Cdd:TIGR02169 944 EE-----------IPEEELSLEDVQAELQRVEEeiralepvnMLAI---QEYE-EVLKRLDELKEKRAKLEEERKAILer 1008
|
....*....
gi 1622833228 4399 -EPLTELKH 4406
Cdd:TIGR02169 1009 iEEYEKKKR 1017
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3552-3654 |
5.47e-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: 42.69 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3552 QFHETAEPISDFLSVTEKKLAnSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLtSPAEQGVLSEKI 3631
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1622833228 3632 DSLQARYSEIQDRCCRKAALLEQ 3654
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
374-452 |
5.69e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 42.29 E-value: 5.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 374 IKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSS 452
Cdd:cd21185 17 VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1662-1852 |
6.77e-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: 45.91 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1662 SEKEKKQISEQLNALNQAYHDLCDGSANQLQQLQSQ----LAHQTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQG 1737
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1738 RTTRQdLSALQKN--QSDLKDL--QDDIQNHATS---FAAVVKDIEGFMEENQTKLSphELTALREKLHQAKEQYEALRE 1810
Cdd:COG4942 105 ELAEL-LRALYRLgrQPPLALLlsPEDFLDAVRRlqyLKYLAPARREQAEELRADLA--ELAALRAELEAERAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622833228 1811 QTRVAQKELEEA-------VTSALQQETEKSKAAKELAENKKKIDALLD 1852
Cdd:COG4942 182 ELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2654-3161 |
8.51e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2654 ERATEVTVARQRQLEESAGHLASFQAAESQLRPwmMEKELmmgvlgplsidpnmlnAQKQQVQFMLKEFEAR-------- 2725
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LEQRL----------------RQQQRAERLLAEFCKRlgknldde 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2726 ------RQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQ-------SINQKWVELTDKLNSRSTQIDQAIVKSTQYQELL 2792
Cdd:PRK04863 554 deleqlQEELEARLESLSESVSEARERRMALRQQLEQLQariqrlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYM 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2793 QDLSEKVRAVGQRLSGqsaISTQPEAVKQQLEETSEIR-SDLEQLdhevkeaQTLCDELS-VLIGEQY----LKDE---- 2862
Cdd:PRK04863 634 QQLLERERELTVERDE---LAARKQALDEEIERLSQPGgSEDPRL-------NALAERFGgVLLSEIYddvsLEDApyfs 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2863 ----------LKKRLETVALPLQGLEDLAAD-----------RMNRLQAAL---ASTQQF-------------------- 2898
Cdd:PRK04863 704 alygparhaiVVPDLSDAAEQLAGLEDCPEDlyliegdpdsfDDSVFSVEElekAVVVKIadrqwrysrfpevplfgraa 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2899 -QQMFDELRTWLDDKQSQQAKNCPISAKLERLHsqlqenEEFQKSLNQHSgsyevivaegeSLLLSVPPGEEKRTLQNQL 2977
Cdd:PRK04863 784 rEKRIEQLRAEREELAERYATLSFDVQKLQRLH------QAFSRFIGSHL-----------AVAFEADPEAELRQLNRRR 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2978 VELKNHWEELSKKTADRQSRLKDCMQKAQKYQWH--------VEDLVPWIEDCKAKMSELRVT-------------LDPV 3036
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQLDEAEEAkrfvqqhgnalaqLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3037 ------------QLESSLLRSKAMLSEVEKRRSLLEILNS---------AADILINSSEADEDgIRDEKAGINQNMDAIT 3095
Cdd:PRK04863 927 vsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSDLNEK-LRQRLEQAEQERTRAR 1005
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 3096 EELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLeifDALGSQACSNKnLEKLRAQQEVLQA 3161
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADSGA-EERARARRDELHA 1067
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1715-1820 |
1.10e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1715 HQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENqtklsPHELTAL 1794
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-----HPDAEEI 75
|
90 100
....*....|....*....|....*.
gi 1622833228 1795 REKLHQAKEQYEALREQTRVAQKELE 1820
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKLE 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2785-3322 |
1.19e-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: 45.48 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2785 STQYQELLQDL----SEKVRAVGQRLSGQS------AISTQPEaVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLI 2854
Cdd:pfam05483 58 DCHYQEGLKDSdfenSEGLSRLYSKLYKEAekikkwKVSIEAE-LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2855 GE--QYLKDELKKR----------LETVALPLQGLEDLAADRMNRLQAALASTQQFQQM---FDELRTwlddkqsqQAKN 2919
Cdd:pfam05483 137 EEeiQENKDLIKENnatrhlcnllKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilaFEELRV--------QAEN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2920 CPISA--KLERLHSQLQE-NEEFQKSLNQHSGSYEVivaegesLLLSVPPGEEK-RTLQNQLVELKNHWEELSKKTADRQ 2995
Cdd:pfam05483 209 ARLEMhfKLKEDHEKIQHlEEEYKKEINDKEKQVSL-------LLIQITEKENKmKDLTFLLEESRDKANQLEEKTKLQD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2996 SRLKDCMQKAQKYQWHVEDLvpwiedckaKMSELRVTLDPVQLESSL-LRSKAMLSEVEKRRSLLEILNSAA---DILIN 3071
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDI---------KMSLQRSMSTQKALEEDLqIATKTICQLTEEKEAQMEELNKAKaahSFVVT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3072 SSEAD----EDGIRDEKAGINQNMDA---ITEELQAKTGSLEEMTQ-------RLKEFQESFKNIEKKVEGAKHQLEIFD 3137
Cdd:pfam05483 353 EFEATtcslEELLRTEQQRLEKNEDQlkiITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3138 ALgsQACSNKNLEKLRAQQEVLQALEPQVD--------YLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQRVNS 3209
Cdd:pfam05483 433 EL--KGKEQELIFLLQAREKEIHDLEIQLTaiktseehYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3210 GCVMMENKLEGIGQFHCRVREMFSQLADLDDEldgmgavgrdTDSLQSQIEDVRL-FLNKIQVVKLDIEASEAECR---- 3284
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEK----------EMNLRDELESVREeFIQKGDEVKCKLDKSEENARsiey 580
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622833228 3285 HMLEEEGTLDLL-----GLKRELEALNKQCGKLTERGKARQEQ 3322
Cdd:pfam05483 581 EVLKKEKQMKILenkcnNLKKQIENKNKNIEELHQENKALKKK 623
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3956-4391 |
1.28e-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: 45.48 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3956 EKTESLIQQYEAiSLLNSERYARLERAQVLVNQfwETYEELSPWIEETRALIAQLPPPA-IDHEQLRQQQEEMRQLRESI 4034
Cdd:pfam05483 222 EKIQHLEEEYKK-EINDKEKQVSLLLIQITEKE--NKMKDLTFLLEESRDKANQLEEKTkLQDENLKELIEKKDHLTKEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4035 AEHKPHIDKLLKIGPQLKE----------LNPEEGEMVEEKYHKAENMYAQIKEEVRQRALALDEAVSQSAQITEFH-DK 4103
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNeDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4104 IEPMLETLENLSSRLR-MPPLI---PAEVDKIRECISDNKSATVELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQ 4179
Cdd:pfam05483 379 LKIITMELQKKSSELEeMTKFKnnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4180 ---DKLDQMVFFWE--DIKARAEEREIKFLDVLELAEKFWYDMAALlttIKDTQDIVHDLESPGIDPSIIKQQVE----A 4250
Cdd:pfam05483 459 ltaIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQEDIINCKKQEErmlkQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4251 AETIKEETDGLHEELEFIR---ILGADLIfACGETEKPEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQ 4327
Cdd:pfam05483 536 IENLEEKEMNLRDELESVReefIQKGDEV-KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622833228 4328 SmfdwlDNTVIKLCTMPPvGTDLNTVKDQLNEMkEFKVEVYQQQIEMEKLNHQGELMLKKATDE 4391
Cdd:pfam05483 615 Q-----ENKALKKKGSAE-NKQLNAYEIKVNKL-ELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2639-3206 |
1.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2639 AENWKKIEEELN--------SRWERATEVTVARQRQLEESAGHLASFQAAESQLrpwmmEKElmmgvlgplsidpnmLNA 2710
Cdd:COG1196 212 AERYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEAELAEL-----EAE---------------LEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2711 QKQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQE 2790
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2791 LLQDLSEKV--------RAVGQRLSGQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELsvligEQYLKDE 2862
Cdd:COG1196 352 ELEEAEAELaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-----EEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2863 LKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKS 2942
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2943 LNQHSGSYEVIVAEGESLLLSVPPGEEKRT-----------LQNQLVE----LKNHWEELSKKTADRQSRL-KDCMQKAQ 3006
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaalaaaLQNIVVEddevAAAAIEYLKAAKAGRATFLpLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3007 KYQWHVEDLVpwiedckakMSELRVTLDPVQLESSLLRSKAMLSEVEkrRSLLEILNSAADILINSSEADEDGIRDEKAG 3086
Cdd:COG1196 587 ALAAALARGA---------IGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3087 INQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLRAQQEVLQALEPQV 3166
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622833228 3167 DYLRNFTQGLVEDAPDGSDASQLLHQAEVTQQEFLEVKQR 3206
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1700-2614 |
1.57e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1700 HQTEQKTLQKQQNTchQQLEDLCSWVG--------QAERALaghQGRTTRQDLSALQKNQS--DLKDLQDDIQNHATSFA 1769
Cdd:TIGR02168 175 KETERKLERTRENL--DRLEDILNELErqlkslerQAEKAE---RYKELKAELRELELALLvlRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1770 AVV---KDIEGFMEENQTKLSPHEL--TALREKLHQAKEQYEALREQTRVAQKELEEAVTSALQQETEKSKAAKELAENK 1844
Cdd:TIGR02168 250 EAEeelEELTAELQELEEKLEELRLevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1845 KKIDALLDWVTSVGSSGGQLLTNLPGM-EQLSKASLEKGTLdttdgymgvNQAPEKLDKHCEKMKARHQELLSQQQhfil 1923
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLeAELEELEAELEEL---------ESRLEELEEQLETLRSKVAQLELQIA---- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1924 ATQSAQAFLDQHGHNLTPEEQQMLQEKLGELKEQYSTSLAQSEAELKQVQTLQDELQKFLQDHREFESWLERSEKELEN- 2002
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQa 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2003 -------MHKGGSSPEALPSLLKRQGSFSEDVIshkgdlrfvtisgqkvldteNSFKEGKEPSEIGNLVKDKLKDATERY 2075
Cdd:TIGR02168 477 ldaaereLAQLQARLDSLERLQENLEGFSEGVK--------------------ALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2076 TALHsecTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEANVGKLLSDTVASDPGVLQQQLATTKQLQEELAEHQVPVEK 2155
Cdd:TIGR02168 537 AAIE---AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2156 LQKVARDIMeiegepapDHKHVQETTDSILShfQSLSYSLAERSSLLQKAIAQSQ-SVQESLESLSQSIGEVEQNLEgkq 2234
Cdd:TIGR02168 614 LRKALSYLL--------GGVLVVDDLDNALE--LAKKLRPGYRIVTLDGDLVRPGgVITGGSAKTNSSILERRREIE--- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2235 vvslssgviqealatnmKLKQDIARQKSSLEATRemvtrfmetadsTTAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKL 2314
Cdd:TIGR02168 681 -----------------ELEEKIEELEEKIAELE------------KALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2315 LPQAEMFEHLSGKLQQFMEnksrmlasgnQPDQDITRFFQQIQELNLEMEDQQENLDTLEhlvtelsscgfaldlsqhqd 2394
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIA----------QLSKELTELEAEIEELEERLEEAEEELAEAE-------------------- 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2395 rvqnlrKDFTELQKTVKEREKDASSCQEQLDEFRKLVRT-----FQKWLKETEGSIPPTETSMSAKELEKQI----EHLK 2465
Cdd:TIGR02168 782 ------AEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERLESLERRIAATERRLEDLEEQIeelsEDIE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2466 SLLDDWASKGTLVEEINCKGTPLENLIMEITAPDSQGKtgsilpsvgssvgsvngyhtcKDLTEIQCDMSDVNLKYEKLG 2545
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLR---------------------SELEELSEELRELESKRSELR 914
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 2546 GILHERQESLQAILNRMEEVQKEANSVLQWLESKEevlkSMDAMSSPTKTETVKAQAESNKAFLAELEQ 2614
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY----SLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3654-4184 |
1.79e-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: 44.94 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3654 QALSNAR-LFGEDEVEVLN---WLAEVEDKLSSV--FVKDFKQ-----DVLHKQHADHLALNEEI---VNRkknvDQAIK 3719
Cdd:COG3096 420 QALEKARaLCGLPDLTPENaedYLAAFRAKEQQAteEVLELEQklsvaDAARRQFEKAYELVCKIageVER----SQAWQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3720 NGQALLKQTTGEEVLLiqEKLDGIKTRYTDItvtsSKALRTLEQARQLATKFQ-------STYEELTGWLREVEEELA-A 3791
Cdd:COG3096 496 TARELLRRYRSQQALA--QRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCqrigqqlDAAEELEELLAELEAQLEeL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3792 SGGQSPTGEQIPQFQQRQKELKKEVMEHRlvldtvnevSRALLelvpWR-AREGLDKL-------VSDANE--------- 3854
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKELA---------ARAPA----WLaAQDALERLreqsgeaLADSQEvtaamqqll 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3855 ----QYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAELAWVAET-KRKLMA-----------------LGPIR---LEQD 3909
Cdd:COG3096 637 ererEATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERlGGVLLSeiyddvtledapyfsalYGPARhaiVVPD 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3910 QTTAQLQVQKAFSID-----IIRHKDSMDE-LFSHRSE----------------------IFGTCGEEQK-TVLQEKTES 3960
Cdd:COG3096 717 LSAVKEQLAGLEDCPedlylIEGDPDSFDDsVFDAEELedavvvklsdrqwrysrfpevpLFGRAAREKRlEELRAERDE 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3961 LIQQY----------------------------------EAISLLNSERY---ARLERAQVLVNQFWETYEELSPWIEET 4003
Cdd:COG3096 797 LAEQYakasfdvqklqrlhqafsqfvgghlavafapdpeAELAALRQRRSeleRELAQHRAQEQQLRQQLDQLKEQLQLL 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4004 RALIAQL----PPPAIDH-EQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKElNPEEGEMVEEKYHKAENMYAQIK- 4077
Cdd:COG3096 877 NKLLPQAnllaDETLADRlEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQS-DPEQFEQLQADYLQAKEQQRRLKq 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 4078 -----EEVRQR--ALALDEAVSQSAQITEFHDKIEPMLETLENLSSRLRmpplipaevDKIRECISDNKSATVELEKLQP 4150
Cdd:COG3096 956 qifalSEVVQRrpHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAR---------EQLRQAQAQYSQYNQVLASLKS 1026
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1622833228 4151 SFEA-------LKRRGEELiGRSQGADKDLAAKEIQDKLDQ 4184
Cdd:COG3096 1027 SRDAkqqtlqeLEQELEEL-GVQADAEAEERARIRRDELHE 1066
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2712-3130 |
1.82e-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: 45.04 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2712 KQQVQFMLKEFEARRQQHEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQEL 2791
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2792 LQDLSEKVRAVGQRL---SGQSAISTQPEAVKQQLEETSEIRSDL-----------EQLDHEVKEAQTLCDELSVLIGE- 2856
Cdd:TIGR00606 614 LESKEEQLSSYEDKLfdvCGSQDEESDLERLKEEIEKSSKQRAMLagatavysqfiTQLTDENQSCCPVCQRVFQTEAEl 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2857 QYLKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDDKQSqqaKNCPISAKLERLHSQLQEN 2936
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRN---KLQKVNRDIQRLKNDIEEQ 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2937 EEFQKSLNQHSGSYEV------IVAEGESLLLSVPPGEEKRTLQNQLVELKNHWEELSKKTADRQSRLKDCMQKAQKYQW 3010
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVcltdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3011 HVEDLVPWIEDCKAKMSELRVtlDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKAGINQN 3090
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKS--EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622833228 3091 MDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAK 3130
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1108-1511 |
1.84e-03 |
|
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: 45.11 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1108 LWHQlhvNTKSLISWNYLRKDLD--LIQTWNLEKLRSSAPGECHQIMKNLQAHcedfLQDSRDSVLFSVADRLRLEEEVE 1185
Cdd:pfam15921 403 LWDR---DTGNSITIDHLRRELDdrNMEVQRLEALLKAMKSECQGQMERQMAA----IQGKNESLEKVSSLTAQLESTKE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1186 ACKAHFQHLM-KSMENEDKEETVAKMYISelknirlrLEEYEqrvvKRIQSLASSRTDRDARQDsaLRIAEQEHTQEDLQ 1264
Cdd:pfam15921 476 MLRKVVEELTaKKMTLESSERTVSDLTAS--------LQEKE----RAIEATNAEITKLRSRVD--LKLQELQHLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1265 QLRSdldaVSMKCDSF-LHQSPSSSSVPTLRSE---LNLLVEKMDHVYGLSTVYLNKLKtvdvivRSIQDAELLVKGYEI 1340
Cdd:pfam15921 542 HLRN----VQTECEALkLQMAEKDKVIEILRQQienMTQLVGQHGRTAGAMQVEKAQLE------KEINDRRLELQEFKI 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1341 KLSQEEAVLADLSA----LEAHRSTLRHWFSD----VKDknsVFSVLDEEIDKAKAVAEQMSRLTPERNLDLERYQEKGS 1412
Cdd:pfam15921 612 LKDKKDAKIRELEArvsdLELEKVKLVNAGSErlraVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1413 QLQERWHRVIAQLEIRQSELESIQEVLGDYRACHGTLIKwIEETTAQQEMMKPGQ--AEDSRVlseQLSQQTALFAEIER 1490
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-VAMGMQKQITAKRGQidALQSKI---QFLEEAMTNANKEK 764
|
410 420
....*....|....*....|.
gi 1622833228 1491 NQTKlDQCQKFSQQYSTIVKD 1511
Cdd:pfam15921 765 HFLK-EEKNKLSQELSTVATE 784
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3006-3106 |
1.97e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3006 QKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQLESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADEDGIRDEKA 3085
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1622833228 3086 GINQNMDAITEELQAKTGSLE 3106
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1980-2090 |
2.05e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1980 QKFLQDHREFESWLERSEKELENMHKGGsSPEALPSLLKRQGSFSEDVISHKGDLRFVTISGQKVLDTENSFKEgkepse 2059
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE------ 73
|
90 100 110
....*....|....*....|....*....|.
gi 1622833228 2060 ignLVKDKLKDATERYTALHSECTRLGFHLN 2090
Cdd:smart00150 74 ---EIEERLEELNERWEELKELAEERRQKLE 101
|
|
| EFh_CREC_RCN3 |
cd16230 |
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ... |
5254-5311 |
2.40e-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: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 5254 FRRIDKDQDGKITRQEFIDGILASKFPTTK-LEMTAVADIFDRDGDGYIDYYEFVAALH 5311
Cdd:cd16230 129 FRVADQDGDSMATREELTAFLHPEEFPHMRdIVVAETLEDLDKNKDGYVQVEEYIADLY 187
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1381-1505 |
3.39e-03 |
|
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: 42.43 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1381 EEIDKAKAVAEQMSRLTPERNLDLERYQEkgsQLQERWHRVIAQLEIRQSELESIQEVLGDYRACHgTLIKWIEETTAQQ 1460
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLE---ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAAL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622833228 1461 EMMKPGQAEDSrvLSEQLSQQTALFAEIERNQTKLDQCQKFSQQY 1505
Cdd:cd00176 130 ASEDLGKDLES--VEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
5476-5650 |
3.60e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5476 PSSPATPASGTKTSLQFSRcYDKPWLVNSKAGTPIRDSHSPDLQLPSPEVISSS--------GSKLKRPTPTFHSSRTSL 5547
Cdd:PHA03307 84 SRSTPTWSLSTLAPASPAR-EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEmlrpvgspGPPPAASPPAAGASPAAV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5548 AGDTSNS---SSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSR-------------RGSDASDFDLLETQSAcSDT 5611
Cdd:PHA03307 163 ASDAASSrqaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisasasspapAPGRSAADDAGASSSD-SSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622833228 5612 SES--SAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGP 5650
Cdd:PHA03307 242 SESsgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2789-3325 |
3.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2789 QELLQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEET----SEIRSDLEQLDHEVKEAQTLCDELSVLIGEQylkDELK 2864
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELEELKEEI---EELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2865 KRLETVALPLQGLEdlaaDRMNRLQAALASTQQFQQMFDELRTWLDDKQSQQAKNCPISAKLERLHSQLQENEEFQKSLN 2944
Cdd:PRK03918 245 KELESLEGSKRKLE----EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2945 QHSGSYEVIVAEGESLllsvppGEEKRTLQNQLVELKNHWEELsKKTADRQSRLKDCMQKAQKYQWHVEDLVPwiEDCKA 3024
Cdd:PRK03918 321 EEINGIEERIKELEEK------EERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTP--EKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3025 KMSELRVTLDPVQLESSLLRSK--AMLSEVEKRRSLLEILNSAADIL-INSSEADEdgirDEKAGInqnMDAITEELQAK 3101
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGKCpVCGRELTE----EHRKEL---LEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3102 TGSLEEMTQRLKEFQESFKNIEKKVEGAKH---QLEIFDALGS--QACSNKNLEKLRAQQEVLQALEPQVDYLRNFTQGL 3176
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESElikLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3177 VEDApdgSDASQLLHQAEVTQQEFLEVKQRVNSgcvmMENKLEGIGqfhcrvremFSQLADLDDELDGMGAVGRDTDSLQ 3256
Cdd:PRK03918 545 KKEL---EKLEELKKKLAELEKKLDELEEELAE----LLKELEELG---------FESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833228 3257 SQIEDVRLFLNKIQVVKLDIEASEAEcrhmLEEEGTlDLLGLKRELEALNKQCGKLTERGKaRQEQLEL 3325
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEE----LAETEK-RLEELRKELEELEKKYSEEEYEEL-REEYLEL 671
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1222-1996 |
3.76e-03 |
|
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: 43.95 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1222 LEEYEQRVvKRIQSLASSRTDRDARQDSALRiaeqehtqEDLQQLRSDLDAVSMKCDSFLH-QSPSSSSVPTLRSELNLL 1300
Cdd:pfam15921 80 LEEYSHQV-KDLQRRLNESNELHEKQKFYLR--------QSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1301 VEKMDHVYGLSTVYLNKLKTvdvivrSIQDAELLVKGYEIKLSQEEAVLADLSALEAHR-------STLrHWFSDVKDKN 1373
Cdd:pfam15921 151 VHELEAAKCLKEDMLEDSNT------QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmSTM-HFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1374 SVFSVLDEEIDKAKA----VAEQMSRLTPERN----LDLERYQEKGSQL-----------QERWHRVIAQLEIRQSELES 1434
Cdd:pfam15921 224 KILRELDTEISYLKGrifpVEDQLEALKSESQnkieLLLQQHQDRIEQLiseheveitglTEKASSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1435 IQEVLGDYRACHGTLIKWIEETTAQ--QEMMKPGQAEDSRVlsEQLSQQTALF-AEIERNQTKLDQcqkFSQQYSTIvkD 1511
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQlrSELREAKRMYEDKI--EELEKQLVLAnSELTEARTERDQ---FSQESGNL--D 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1512 YELQLMT---YKAFVE-SQQKSPGKRRRMLSSSDAITQEFM--DLRTRytalvtltTQHVKYISDALRRLEEEEKVVEEE 1585
Cdd:pfam15921 377 DQLQKLLadlHKREKElSLEKEQNKRLWDRDTGNSITIDHLrrELDDR--------NMEVQRLEALLKAMKSECQGQMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1586 KQEHVEKVKELLGWVSTLarntqgkatsSQTKESTdieKAILEQQVlaEELTTKKEQVSEAIKTSQIFLAkhghklSEKE 1665
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSL----------TAQLEST---KEMLRKVV--EELTAKKMTLESSERTVSDLTA------SLQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1666 KKQISEQLNALNQAYHDLCDGSANQLQQLQSQLAH----QTEQKTLQKQQ-------NTCHQQLEDLCSWVGQaeralag 1734
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHlrnvQTECEALKLQMaekdkviEILRQQIENMTQLVGQ------- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1735 hQGRTTrqdlSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENQTKLSPHELTALReKLHQAKEQYEALREQTRV 1814
Cdd:pfam15921 581 -HGRTA----GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK-LVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1815 AQKELEEAVTS--ALQQETEKSKAAKELAENKkkidalldwvtsvgSSGGQLLTNLPGMEQLSKASLEKGTLDTTdgymg 1892
Cdd:pfam15921 655 RDQLLNEVKTSrnELNSLSEDYEVLKRNFRNK--------------SEEMETTTNKLKMQLKSAQSELEQTRNTL----- 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1893 vnQAPEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHGHNLTpEEQQMLQEKLGELKEQYSTSLAQSEAELKQV 1972
Cdd:pfam15921 716 --KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN-KEKHFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
810 820
....*....|....*....|....
gi 1622833228 1973 QTLQDELQKFLQDHREFESWLERS 1996
Cdd:pfam15921 793 EVLRSQERRLKEKVANMEVALDKA 816
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3627-4083 |
4.50e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3627 LSEKIDSLQARYSEIQDRccrkaalLEQALSNARLFGEDEVEVLNWLAEVEDKLSSVfvkdfkQDVLHKQHADHLALNEE 3706
Cdd:PRK02224 277 LAEEVRDLRERLEELEEE-------RDDLLAEAGLDDADAEAVEARREELEDRDEEL------RDRLEECRVAAQAHNEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3707 IVNRKKNVDQA------IKNGQALLK---QTTGEEV-------LLIQEKLDGIKTRYTDITVTSSKA-------LRTLEQ 3763
Cdd:PRK02224 344 AESLREDADDLeeraeeLREEAAELEselEEAREAVedrreeiEELEEEIEELRERFGDAPVDLGNAedfleelREERDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3764 ARQLATKFQSTYEELTGWLREVEEELAASG----GQ----SPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLE 3835
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEAGKcpecGQpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3836 LVPWRARegldklVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADaELAWVAETKRKLMALGPIRLEQD-QTTAQ 3914
Cdd:PRK02224 504 LVEAEDR------IERLEERREDLEELIAERRETIEEKRERAEELRERAA-ELEAEAEEKREAAAEAEEEAEEArEEVAE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3915 LQVQKAFSIDIIRHKDSMDELFSHRSEifgtcgeeqktvLQEKTESLIQQYEAISLLNSERYARL----ERAQVLVNQFW 3990
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIAD------------AEDEIERLREKREALAELNDERRERLaekrERKRELEAEFD 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3991 ET-YEELSPWIEETRALIAQLpppaidHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNpEEGEMVEEKYHKA 4069
Cdd:PRK02224 645 EArIEEAREDKERAEEYLEQV------EEKLDELREERDDLQAEIGAVENELEELEELRERREALE-NRVEALEALYDEA 717
|
490
....*....|....*..
gi 1622833228 4070 E---NMYAQIKEEVRQR 4083
Cdd:PRK02224 718 EeleSMYGDLRAELRQR 734
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
5476-5650 |
4.76e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5476 PSSPATPASGTKTSLQFSRcydkpwlvnSKAGTPIRDSHSPdlqlPSPEViSSSGSKLKRPTPTFHSSRTSLAGDTSNSS 5555
Cdd:PHA03307 266 PTRIWEASGWNGPSSRPGP---------ASSSSSPRERSPS----PSPSS-PGSGPAPSSPRASSSSSSSRESSSSSTSS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5556 SPASTGAKTnrADPKKSASRPGSRAGSRAGSRASSRRGSDASDfDLLETQSACSDTSESSAAGGQ---------GNSRRG 5626
Cdd:PHA03307 332 SSESSRGAA--VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS-RAPSSPAASAGRPTRRRARAAvagrarrrdATGRFP 408
|
170 180
....*....|....*....|....
gi 1622833228 5627 LNKPSKIPTmSKKTTTASPRTPGP 5650
Cdd:PHA03307 409 AGRPRPSPL-DAGAASGAFYARYP 431
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2637-3448 |
4.79e-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: 43.50 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2637 QEAENWKKIEEELNSRWERATEVTVARQRQLEESAGHLASFQAAESQLRPWMMEKELMMGVLGPLSIDPNMLNAQKQQVQ 2716
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2717 FMLKEFEARRQQ-----HEQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVEltdkLNSRSTQIDQAIVKSTQYQEL 2791
Cdd:TIGR00606 283 KDNSELELKMEKvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL----LNQEKTELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2792 LQDLSEKVRAVGQRLSGQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDEL-SVLIGEQYLKDELKKRLETV 2870
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLqSKERLKQEQADEIRDEKKGL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2871 ALPLQGLEDLAADRMNRL-------QAALASTQQFQQMFDELRTWLDDkQSQQAKNCPISAKLERLHSQLQENEEFQKSL 2943
Cdd:TIGR00606 439 GRTIELKKEILEKKQEELkfvikelQQLEGSSDRILELDQELRKAERE-LSKAEKNSLTETLKKEVKSLQNEKADLDRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2944 NQHSGSYEVIVAEGESLLLSVPPGEEKRTLQNQLVELK-NHWEELS-----------------------KKTADRQSRLK 2999
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTsllgyfpnkkqledwlhskskeiNQTRDRLAKLN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3000 DCMQKAQKYQWHVEDLVPWIEDCKAKMSELRVTLDPVQ-LESSLLRSKAMLSEVEKRRSLLEILNSAADILINSSEADED 3078
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3079 GIrdekAGINQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLeifdalgsqacsnknLEKLRAQQEV 3158
Cdd:TIGR00606 678 SC----CPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM---------------LGLAPGRQSI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3159 LQALEPQVDYLRNFTQGLVED-APDGSDASQLLHQAEVTQQEfLEVKQRVNSGCVMMENKLEGIGQfhcrVREMFSQLAD 3237
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDiQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKD----VERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3238 LDDELDGMGAVGRDTDSLQSQIEDVRLFLNKIQVVKLDIEASEAECRHMleeEGTLDLLGLKRelealnKQCGKLTERGK 3317
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL---KSKTNELKSEK------LQIGTNLQRRQ 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3318 ARQEQLELTLGRVEDFYRKLKglNDATTAAEEAEALQWVVGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLI 3397
Cdd:TIGR00606 885 QFEEQLVELSTEVQSLIREIK--DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-VNDIKEKVKNIHGYMKDIE 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1622833228 3398 QSAGKDCDVQGLEHDMEeinarwntlnkkVAQRIAQLQEALLHCGKFQDAL 3448
Cdd:TIGR00606 962 NKIQDGKDDYLKQKETE------------LNTVNAQLEECEKHQEKINEDM 1000
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2140-2793 |
5.08e-03 |
|
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: 43.57 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2140 KQLQEELAEHQVPVEKLQKVARDIMEIEGEPAPDHKHVQETtdsilsHFQSLSYSLA--------ERSSL---------- 2201
Cdd:pfam15921 173 EQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFRSLGSAISkilreldtEISYLkgrifpvedq 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2202 LQKAIAQSQS-----VQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNMKLKQDIARQKSSleatreMVTRFME 2276
Cdd:pfam15921 247 LEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS------MYMRQLS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2277 TADSTTAAvLQGKLAEVSQRFEQlclQQQEKESSLkkLLPQAEMFEHLSGKlQQFMENksrmlaSGNQPDQD---ITRFF 2353
Cdd:pfam15921 321 DLESTVSQ-LRSELREAKRMYED---KIEELEKQL--VLANSELTEARTER-DQFSQE------SGNLDDQLqklLADLH 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2354 QQIQELNLEMEDQQENLD-------TLEHLVTELSscgfalDLSQHQDRVQNLRKDFTELQKTVKEREKDA--------- 2417
Cdd:pfam15921 388 KREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELD------DRNMEVQRLEALLKAMKSECQGQMERQMAAiqgknesle 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2418 --SSCQEQLDEFRKLVRTFQKWLketegsippTETSMSAKELEKQIEHLKSLLDDwasKGTLVEEINCKGTPLENLI-ME 2494
Cdd:pfam15921 462 kvSSLTAQLESTKEMLRKVVEEL---------TAKKMTLESSERTVSDLTASLQE---KERAIEATNAEITKLRSRVdLK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2495 ITAPDSQGKTGSILPSVGSSVGSVNGYHTCKDLT------EIQCDMSDVNLKYEKLGGILHERQESLQAILNRMEEVQKe 2568
Cdd:pfam15921 530 LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2569 ansvLQWLESKEEV-LKSMDAMSSPTKTETVK---AQAESNKA---FLAELEQNSPKIQKVKEALAGLLVTYPNSQEaeN 2641
Cdd:pfam15921 609 ----FKILKDKKDAkIRELEARVSDLELEKVKlvnAGSERLRAvkdIKQERDQLLNEVKTSRNELNSLSEDYEVLKR--N 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2642 WKKIEEELNSRWERATEVTVARQRQLEESAGHLASFQAAESQlrpwmmEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKE 2721
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH------AMKVAMGMQKQITAKRGQIDALQSKIQFLEEA 756
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622833228 2722 F-EARRQQH---EQLNEAAQGILTgpgdVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKSTQYQELLQ 2793
Cdd:pfam15921 757 MtNANKEKHflkEEKNKLSQELST----VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2710-3273 |
5.48e-03 |
|
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: 43.57 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2710 AQKQQVQFMLKEFEARRQQH---EQLNEAAQGILTGPGDVSLSTSQVQKELQSINQKWVELTDKLNSRSTQIDQAIVKS- 2785
Cdd:pfam15921 294 ANSIQSQLEIIQEQARNQNSmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2786 ---TQYQELLQDLSEKvravgqrlsgQSAISTQPEAVKQQLEETSEIRSDLEQLDHEVKEAQTLCDELSVLIgeQYLKDE 2862
Cdd:pfam15921 374 nldDQLQKLLADLHKR----------EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL--KAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2863 LKKRLETVALPLQGlEDLAADRMNRLQAALASTQQ-FQQMFDEL-----------RTWLDDKQSQQAKNCPISA---KLE 2927
Cdd:pfam15921 442 CQGQMERQMAAIQG-KNESLEKVSSLTAQLESTKEmLRKVVEELtakkmtlesseRTVSDLTASLQEKERAIEAtnaEIT 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2928 RLHSQLQENEEFQKSLNQHSGSYEVIVAEGESLLLSVppgeekrTLQNQLVELKNHWEELSKKTADRQSRLKDCMQkAQK 3007
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQM-------AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ-VEK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3008 YQWHVEdlvpwIEDCKAKMSELRVTLDpvqlessllRSKAMLSEVEKRRSLLEILNSAadiLINSSEADEDGIRDekagI 3087
Cdd:pfam15921 593 AQLEKE-----INDRRLELQEFKILKD---------KKDAKIRELEARVSDLELEKVK---LVNAGSERLRAVKD----I 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3088 NQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEI------------FDALGSQACSNKNLEKLR-A 3154
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqlksaqseleqtRNTLKSMEGSDGHAMKVAmG 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3155 QQEVLQALEPQVDYLRNFTQGLVEDAPDGSDASQLLHQAEVT-QQEFLEVKQRVNSgcvmMENKLEGIGQFHCRVREMFS 3233
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlSQELSTVATEKNK----MAGELEVLRSQERRLKEKVA 807
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622833228 3234 QLADLDDELDGMGAVGRDTDSLQSQiEDVRLFLNKIQVVK 3273
Cdd:pfam15921 808 NMEVALDKASLQFAECQDIIQRQEQ-ESVRLKLQHTLDVK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1634-2265 |
6.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1634 EELTTKKEQVSEAIKTSQIFLAKHGHKLSEKEKK--QISEQLNALNQAYHDLcdgsanqlqqlqsqLAHQTEQKTLQKQQ 1711
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSElpELREELEKLEKEVKEL--------------EELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1712 NTCHQQLEDLCSWVGQAERALAGhqgrtTRQDLSALQKNQSDLKDLQDDIQNHATsfaavvkdIEGFMEEnqtklsphel 1791
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKELKELKEKAEEYIK--------LSEFYEE---------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1792 taLREKLHQAKEQYEALREQTRVAQKELEEAVtsalQQETEKSKAAKELAENKKKIDALLDWVTSVgSSGGQLLTNlpgM 1871
Cdd:PRK03918 305 --YLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEE---L 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1872 EQLSKASLEKGTLDTTDGYMGVNQAPEKLDKHCEKMKARHQEL---LSQQQHFILATQSAQAFLDQHGHNLTPEEQqmlq 1948
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELkkeIKELKKAIEELKKAKGKCPVCGRELTEEHR---- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1949 eklGELKEQYSTSLAQSEAELKqvqTLQDELQKFLQDHREFESWLERsEKELENMHKggsSPEALPSLLKRQGSFSEDVI 2028
Cdd:PRK03918 451 ---KELLEEYTAELKRIEKELK---EIEEKERKLRKELRELEKVLKK-ESELIKLKE---LAEQLKELEEKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2029 SHKGDL------RFVTISGQkVLDTENSFKEGKEPSEIGNLVKDKLKDATERYTALHSECTRLGFhlnmllgqyhqfqNS 2102
Cdd:PRK03918 521 EKKAEEyeklkeKLIKLKGE-IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF-------------ES 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2103 ADSLQAWMQTCEANVGKLLSdtVASDPGVLQQQLATTKQLQEELAEHQvpvEKLQKVARDIMEIEGEPAPDHKHVQETTd 2182
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAF---EELAETEKRLEELRKELEELEKKYSEEE- 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2183 silshFQSLSYSLAERSSLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQVVSLSSGVIQEALATNMKLKQDIARQKS 2262
Cdd:PRK03918 661 -----YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
...
gi 1622833228 2263 SLE 2265
Cdd:PRK03918 736 LLK 738
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3357-3436 |
6.15e-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: 39.61 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 3357 VGTEVEIINQQLADFKMFQKEqVDPLQMKLQQVNGLGQGLIQSAGKDCDVqgLEHDMEEINARWNTLNKKVAQRIAQLQE 3436
Cdd:pfam00435 29 YGKDLESVQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2120-2374 |
6.24e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2120 LLSDTVASDPGVLQQQLATTKQLQEELAEHQvpvEKLQKVARDImeiegepapdhkhvqettDSILSHFQSLSYSLAERS 2199
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELE---KELAALKKEE------------------KALLKQLAALERRIAALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2200 SLLQKAIAQSQSVQESLESLSQSIGEVEQNLEGKQvvslssGVIQEALATNMKLKQD-----IARQKSSLEATRE-MVTR 2273
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQK------EELAELLRALYRLGRQpplalLLSPEDFLDAVRRlQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2274 FMETADSTTAAVLQGKLAEVSQRFEQLCLQQQEKESSLKKLLPQAEmfehlsgKLQQFMENKSRMLAsgnQPDQDITRFF 2353
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-------ALEALKAERQKLLA---RLEKELAELA 212
|
250 260
....*....|....*....|.
gi 1622833228 2354 QQIQELNLEMEDQQENLDTLE 2374
Cdd:COG4942 213 AELAELQQEAEELEALIARLE 233
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
5223-5274 |
6.68e-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: 38.30 E-value: 6.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622833228 5223 ELKE-FANFDFD----VWRKKYMRWMNH-----KKSRVMDFFRRIDKDQDGKITRQEFIDGI 5274
Cdd:cd00051 1 ELREaFRLFDKDgdgtISADELKAALKSlgeglSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1663-1852 |
7.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1663 EKEKKQISEQLNALNQAYHDLcdgsanqlqqlqsqlahQTEQKTLQKQQNTCHQQLEDLCSWVGQAERALAGHQGRTTRQ 1742
Cdd:COG3883 29 QAELEAAQAELDALQAELEEL-----------------NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1743 dLSALQKNQSDLKDLqdDIQNHATSFAAVVKDIEG---FMEENQTKLSphELTALREKLHQAKEQYEALREQTRVAQKEL 1819
Cdd:COG3883 92 -ARALYRSGGSVSYL--DVLLGSESFSDFLDRLSAlskIADADADLLE--ELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|...
gi 1622833228 1820 EEAVTSALQQETEKSKAAKELAENKKKIDALLD 1852
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| EFh_PEF_Group_I |
cd16180 |
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
5249-5311 |
8.22e-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: 40.59 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 5249 RVMDFFRRIDKDQDGKITRQEF-------------IDGI--LASKFPTT---KLEMT-------------AVADIFDRDG 5297
Cdd:cd16180 1 ELRRIFQAVDRDRSGRISAKELqralsngdwtpfsIETVrlMINMFDRDrsgTINFDefvglwkyiqdwrRLFRRFDRDR 80
|
90
....*....|....
gi 1622833228 5298 DGYIDYYEFVAALH 5311
Cdd:cd16180 81 SGSIDFNELQNALS 94
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1715-1959 |
8.76e-03 |
|
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: 41.28 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1715 HQQLEDLCSWVGQAERALAGHQgrtTRQDLSALQKNQSDLKDLQDDIQNHATSFAAVVKDIEGFMEENqtklsPHELTAL 1794
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1795 REKLHQAKEQYEALREQTRVAQKELEEAVtsalqqetekskaakELAENKKKIDALLDWVTSVgssggqlltnlpgMEQL 1874
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEAL---------------DLQQFFRDADDLEQWLEEK-------------EAAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1875 SKASLEKgtldttdgymgvnqAPEKLDKHCEKMKARHQELLSQQQHFILATQSAQAFLDQHGHNLTPEeqqmLQEKLGEL 1954
Cdd:cd00176 130 ASEDLGK--------------DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE----IEEKLEEL 191
|
....*
gi 1622833228 1955 KEQYS 1959
Cdd:cd00176 192 NERWE 196
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1942-2300 |
9.24e-03 |
|
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: 42.80 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1942 EEQQMLQEKLGELKEQY---STSLAQSEAELKQVQ----TLQDELQKFLQD--HREFESWLERSE--------------- 1997
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLvlaNSELTEARTERDQFSqesgNLDDQLQKLLADlhKREKELSLEKEQnkrlwdrdtgnsiti 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 1998 ----KELENMHKGGSSPEALPSLLKR--QGSFS-------------EDVISHKGDLRFVTISGQKVLDTENSFKEGKEPS 2058
Cdd:pfam15921 415 dhlrRELDDRNMEVQRLEALLKAMKSecQGQMErqmaaiqgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2059 E--IGNLVKdKLKDATERYTALHSECTRLGFHLNMLLGQYHQFQNSADSLQAWMQTCEA---------NVGKLLSDTVAS 2127
Cdd:pfam15921 495 ErtVSDLTA-SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlklqmaekdKVIEILRQQIEN 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2128 DPGVLQQQ-------LATTKQLQEELAEHQVPVEKLqKVARD-----IMEIEGEPAPDHKHVQETTDSILSHFQSLSYSL 2195
Cdd:pfam15921 574 MTQLVGQHgrtagamQVEKAQLEKEINDRRLELQEF-KILKDkkdakIRELEARVSDLELEKVKLVNAGSERLRAVKDIK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833228 2196 AERSSLLQKAiaqsQSVQESLESLSQSIGEVEQNLEGKQvvslssgviQEALATNMKLKQDIARQKSSLEATREMVtRFM 2275
Cdd:pfam15921 653 QERDQLLNEV----KTSRNELNSLSEDYEVLKRNFRNKS---------EEMETTTNKLKMQLKSAQSELEQTRNTL-KSM 718
|
410 420
....*....|....*....|....*
gi 1622833228 2276 ETADSTTAAVLQGKLAEVSQRFEQL 2300
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
5249-5274 |
9.27e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 36.77 E-value: 9.27e-03
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
5249-5274 |
9.41e-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: 9.41e-03
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