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Conserved domains on  [gi|542133174|ref|NP_001269465|]
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liprin-alpha-2 isoform j [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
951-1022 7.87e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 7.87e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  951 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1022
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
742-812 2.74e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 2.74e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542133174  742 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 812
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
866-931 4.05e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 4.05e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174  866 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 931
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
209-383 1.01e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  209 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 276
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 346
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 542133174  347 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 383
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
T4SS super family cl19516
Type IV secretion system proteins; Members of this family are components of the type IV ...
131-244 4.50e-03

Type IV secretion system proteins; Members of this family are components of the type IV secretion system. They mediate intracellular transfer of macromolecules via a mechanism ancestrally related to that of bacterial conjugation machineries.


The actual alignment was detected with superfamily member pfam07996:

Pssm-ID: 267869  Cd Length: 195  Bit Score: 38.48  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   131 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME-------ERITTLEKryLSAQREST- 202
Cdd:pfam07996   72 YDLVLDGYGGLSSSAKSLYSKEKLFDTCSYPSGSRASICQRSADKAAQDKAVGEqaydqatNRLSQIEQ--LRSQIDSAk 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 542133174   203 ---SIHDMNDKLENELA--NKEAILRQMEEKNRQLQERLElAEQKLQ 244
Cdd:pfam07996  150 dpkEIADLQARIQAEQAmlQNEQTKLQMLQMLQEAEERLE-EQQAAE 195
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
742-808 7.72e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


:

Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 53.84  E-value: 7.72e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174    742 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 808
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
952-1023 8.20e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


:

Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 8.20e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174    952 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1023
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
52-348 3.62e-04

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


:

Pssm-ID: 259052 [Multi-domain]  Cd Length: 305  Bit Score: 42.38  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    52 LEEELAAANQEIVALREQNVHIQRKMaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE----TSQIVELQELLEKQ 127
Cdd:pfam14915    4 LQDEIAMLRLEIDTIKNQNQEKEKKY-FEDIKILKEKNDDLQKTIKLNEETLTKTVFQYSGQlnvlKAENTMLNSKLENE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   128 NYEMAQMKERLAALSSRVGEVEQEAE---TARKDLIKTeemntkYQRDIREAMAQKEDMEERITTLEkrylsaqrestsi 204
Cdd:pfam14915   83 KQNKERLETEVESYRSRLAAAIQDHEqsqTSKRDLELA------FQRARDEWLRLQDKMNFDVSNLK------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   205 hDMNDKLENELANKEAILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEER 280
Cdd:pfam14915  144 -DNNEVLSQQLSKAESKFNSLEIELHHTRDALRektLLLEHVQRDLSQAQCqKKEIEHMYQNEQGKVSKYMGKQESLEER 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174   281 MRHLEGQLEEKNQELQRARQR----EKMNEEHNKRLSDTVDRLLTESnERLQLHLKERMAALEEKNVLIQES 348
Cdd:pfam14915  223 LSQLQSENLLLRQQLDDAQNKgdskEKTVINIQDQFQDILKKLQAES-EKQVLLLEERNKELMKECNHLKER 293
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
874-929 1.55e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


:

Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 1.55e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174    874 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 929
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
951-1022 7.87e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 7.87e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  951 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1022
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
742-812 2.74e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 2.74e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542133174  742 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 812
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
866-931 4.05e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 4.05e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174  866 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 931
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
865-929 2.85e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 249940  Cd Length: 64  Bit Score: 63.80  E-value: 2.85e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   865 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 929
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYADNFRAGYIDGDALLLLTEEDLE-KLGVTLPGHRKKILSSIQGLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
952-1022 9.96e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 254328  Cd Length: 66  Bit Score: 41.88  E-value: 9.96e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542133174   952 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1022
Cdd:pfam07647    1 VESWSLEDVAEWLRSIGLPQYADNFRDQGITGaeLLLRLTEED-------LKALGITSVGHRRKILKKIQRLK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
209-383 1.01e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  209 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 276
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 346
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 542133174  347 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 383
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
744-808 1.13e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 249940  Cd Length: 64  Bit Score: 41.46  E-value: 1.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   744 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIQReIGISNPLHRLKLRLAIQEM 808
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YADNFRAGYIDGDALLLLTEEDLEK-LGVTLPGHRKKILSSIQGL 63
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and ...
232-373 2.22e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpmlp spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tmp3 members.


Pssm-ID: 257245  Cd Length: 143  Bit Score: 41.43  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   232 LQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 311
Cdd:pfam12718   12 AQERAEELEEKLKELEQENL-------EKEQEIKSLQK---KNQQLEEEVEKLEEQLKEAKEKLEESEKLATNAEALTRR 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542133174   312 LsdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE-ESLHDKERLAEEIEKLR 373
Cdd:pfam12718   82 I-----QLLEEELEESEKRLKETTEKLREADKKAEESERKVKALEnERDEWEEKYEELEKKYK 139
T4SS pfam07996
Type IV secretion system proteins; Members of this family are components of the type IV ...
131-244 4.50e-03

Type IV secretion system proteins; Members of this family are components of the type IV secretion system. They mediate intracellular transfer of macromolecules via a mechanism ancestrally related to that of bacterial conjugation machineries.


Pssm-ID: 254572  Cd Length: 195  Bit Score: 38.48  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   131 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME-------ERITTLEKryLSAQREST- 202
Cdd:pfam07996   72 YDLVLDGYGGLSSSAKSLYSKEKLFDTCSYPSGSRASICQRSADKAAQDKAVGEqaydqatNRLSQIEQ--LRSQIDSAk 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 542133174   203 ---SIHDMNDKLENELA--NKEAILRQMEEKNRQLQERLElAEQKLQ 244
Cdd:pfam07996  150 dpkEIADLQARIQAEQAmlQNEQTKLQMLQMLQEAEERLE-EQQAAE 195
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
742-808 7.72e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 53.84  E-value: 7.72e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174    742 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 808
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
952-1023 8.20e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 8.20e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174    952 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1023
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
52-348 3.62e-04

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 259052 [Multi-domain]  Cd Length: 305  Bit Score: 42.38  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    52 LEEELAAANQEIVALREQNVHIQRKMaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE----TSQIVELQELLEKQ 127
Cdd:pfam14915    4 LQDEIAMLRLEIDTIKNQNQEKEKKY-FEDIKILKEKNDDLQKTIKLNEETLTKTVFQYSGQlnvlKAENTMLNSKLENE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   128 NYEMAQMKERLAALSSRVGEVEQEAE---TARKDLIKTeemntkYQRDIREAMAQKEDMEERITTLEkrylsaqrestsi 204
Cdd:pfam14915   83 KQNKERLETEVESYRSRLAAAIQDHEqsqTSKRDLELA------FQRARDEWLRLQDKMNFDVSNLK------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   205 hDMNDKLENELANKEAILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEER 280
Cdd:pfam14915  144 -DNNEVLSQQLSKAESKFNSLEIELHHTRDALRektLLLEHVQRDLSQAQCqKKEIEHMYQNEQGKVSKYMGKQESLEER 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174   281 MRHLEGQLEEKNQELQRARQR----EKMNEEHNKRLSDTVDRLLTESnERLQLHLKERMAALEEKNVLIQES 348
Cdd:pfam14915  223 LSQLQSENLLLRQQLDDAQNKgdskEKTVINIQDQFQDILKKLQAES-EKQVLLLEERNKELMKECNHLKER 293
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
36-380 5.31e-19

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 91.70  E-value: 5.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmassegstesehLEGMEPGQKVHEKRLSNGSIDSTDETS 115
Cdd:COG1196   670 KELEEELAELEAQLEKLEEELKSLKNELRSLEDL-------------------LEELRRQLEELERQLEELKRELAALEE 730
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 195
Cdd:COG1196   731 ELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLD 810
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHG 275
Cdd:COG1196   811 ALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELE---ELEAEKEELEDELKELEEEKE 887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  276 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQL-----------HLKERMAALEEKNVL 344
Cdd:COG1196   888 ELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDtletelereieRLEEEIEALGPVNLR 967
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 542133174  345 -IQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:COG1196   968 aIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELD 1004
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-381 6.15e-16

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 6.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 193
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   194 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 273
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   274 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 349
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270
                   ....*....|....*....|....*....|..
gi 542133174   350 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
PRK02224 PRK02224
chromosome segregation protein; Provisional
18-435 1.07e-12

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.22  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   18 VEVLKALKSLFEHHkaldEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEpgqk 97
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEERDDLLAEAG---- 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   98 vhekrLSNGSIDSTDE-----TSQIVELQELLEKQ-------NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEm 165
Cdd:PRK02224  304 -----LDDADAEAVEArreelEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEARE- 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  166 ntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqq 245
Cdd:PRK02224  378 ------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA---- 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  246 tMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLT 321
Cdd:PRK02224  448 -LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIA 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  322 ESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSA 400
Cdd:PRK02224  527 ERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIA 602
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 542133174  401 ELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 435
Cdd:PRK02224  603 DAEDEIERLREKREALAE---LNDERRERLAEKRE 634
PTZ00121 PTZ00121
MAEBL; Provisional
32-361 4.33e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   32 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRlsngsidST 111
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKK-------KA 1548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLE 191
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  192 KRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQ 262
Cdd:PTZ00121 1625 LK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAK 1702
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  263 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
                         330       340
                  ....*....|....*....|..
gi 542133174  340 EKnvLIQESETFRKNLEESLHD 361
Cdd:PTZ00121 1783 EE--LDEEDEKRRMEVDKKIKD 1802
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
874-929 1.55e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 1.55e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174    874 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 929
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
226-532 1.79e-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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   226 EEKNRQLQ----ERLELAE-QKLQQTMRKAET---LPEVEAELAQRIAALTKAEErhgnIEERMRHLEGQLEEKNQELQR 297
Cdd:TIGR02169  194 DEKRQQLErlrrEREKAERyQALLKEKREYEGyelLKEKEALERQKEAIERQLAS----LEEELEKLTEEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   298 ARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHdkeRLAEEIEKLRSELD 377
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID---KLLAEIEELEREIE 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   378 QLKMRTGSLIEPTIP-RTHLDTS----AELRYSVGSLVDSQSDYRT--TKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRT 450
Cdd:TIGR02169  347 EERKRRDKLTEEYAElKEELEDLraelEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQRLSEELADLN 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   451 QQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAINKEIRLIQEEKESTELRAEEIEN 530
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVEKELSKLQRELAEAEAQARASEE 504

                   ..
gi 542133174   531 RV 532
Cdd:TIGR02169  505 RV 506
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
333-391 3.40e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 3.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  333 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 391
Cdd:PRK03992    1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
zf-C4H2 pfam10146
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
286-395 1.14e-03

Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumor-associated antigen HCA127 in humans but this could not confirmed.


Pssm-ID: 204405 [Multi-domain]  Cd Length: 215  Bit Score: 40.22  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   286 GQLEEKNQELQRARQREKMNEEHnkrlSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERL 365
Cdd:pfam10146    4 KEIRNKTDELEKLKDEIKAEEEA----LESEEKHLKEYDKEMEELLEEKMQHVEELRQIHADINDMETEIKQSKSELERR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 542133174   366 AEEIEKLRSELDQLK-----MRTGSLIEPTIPRTH 395
Cdd:pfam10146   80 MGKIARMHGEYNPLKesineMRKLELGLEELPQLH 114
46 PHA02562
endonuclease subunit; Provisional
59-274 2.21e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   59 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 126
Cdd:PHA02562  179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  127 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 197
Cdd:PHA02562  253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542133174  198 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 274
Cdd:PHA02562  333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
134-402 7.80e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 38.68  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  134 MKERlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK--EDMEERITT------LEKRYLSAqRESTSIH 205
Cdd:PLN03229  421 MKKR-EAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKlkKEIDLEYTEaviamgLQERLENL-REEFSKA 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  206 DMNDKLENElANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKaeERHGNIEERMRHLE 285
Cdd:PLN03229  499 NSQDQLMHP-VLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKA--EINKKFKEVMDRPE 575
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  286 gqLEEKNQELQRARQREKMNEEhnkrlsDTVDRLLTESNERLQLHLKERMA-ALEEKNVLIQESETFRKNLEESLHDKEr 364
Cdd:PLN03229  576 --IKEKMEALKAEVASSGASSG------DELDDDLKEKVEKMKKEIELELAgVLKSMGLEVIGVTKKNKDTAEQTPPPN- 646
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 542133174  365 LAEEIEKLRSEldqlkmrTGSLIEPTIPRTHLDTSAEL 402
Cdd:PLN03229  647 LQEKIESLNEE-------INKKIERVIRSSDLKSKIEL 677
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
951-1022 7.87e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.40  E-value: 7.87e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  951 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1022
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
742-812 2.74e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 153.10  E-value: 2.74e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542133174  742 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 812
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
866-931 4.05e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 4.05e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174  866 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 931
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
870-929 6.80e-31

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 117.25  E-value: 6.80e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  870 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 929
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
749-807 1.30e-26

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.00  E-value: 1.30e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 542133174  749 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 807
Cdd:cd09494     1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
959-1020 2.08e-24

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 98.77  E-value: 2.08e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  959 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1020
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
951-1022 4.00e-18

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 80.95  E-value: 4.00e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  951 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1022
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
743-807 1.31e-16

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 76.72  E-value: 1.31e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174  743 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 807
Cdd:cd09564     2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
865-929 4.03e-16

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 75.04  E-value: 4.03e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174  865 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 929
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
865-929 4.67e-16

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 74.75  E-value: 4.67e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174  865 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 929
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
951-1022 5.36e-15

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.10  E-value: 5.36e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  951 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1022
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
865-929 2.85e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 249940  Cd Length: 64  Bit Score: 63.80  E-value: 2.85e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   865 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 929
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYADNFRAGYIDGDALLLLTEEDLE-KLGVTLPGHRKKILSSIQGLK 64
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
742-806 3.49e-12

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 63.79  E-value: 3.49e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174  742 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 806
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
874-925 1.01e-05

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886  Cd Length: 56  Bit Score: 44.54  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 542133174  874 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 925
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
952-1022 9.96e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 254328  Cd Length: 66  Bit Score: 41.88  E-value: 9.96e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542133174   952 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1022
Cdd:pfam07647    1 VESWSLEDVAEWLRSIGLPQYADNFRDQGITGaeLLLRLTEED-------LKALGITSVGHRRKILKKIQRLK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
209-383 1.01e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  209 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 276
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 346
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 542133174  347 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 383
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
744-808 1.13e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 249940  Cd Length: 64  Bit Score: 41.46  E-value: 1.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   744 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIQReIGISNPLHRLKLRLAIQEM 808
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YADNFRAGYIDGDALLLLTEEDLEK-LGVTLPGHRKKILSSIQGL 63
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and ...
232-373 2.22e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpmlp spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tmp3 members.


Pssm-ID: 257245  Cd Length: 143  Bit Score: 41.43  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   232 LQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 311
Cdd:pfam12718   12 AQERAEELEEKLKELEQENL-------EKEQEIKSLQK---KNQQLEEEVEKLEEQLKEAKEKLEESEKLATNAEALTRR 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542133174   312 LsdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE-ESLHDKERLAEEIEKLR 373
Cdd:pfam12718   82 I-----QLLEEELEESEKRLKETTEKLREADKKAEESERKVKALEnERDEWEEKYEELEKKYK 139
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
745-803 4.65e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 39.62  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  745 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 803
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
121-299 5.61e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  121 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 200
Cdd:cd00176    64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  201 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 280
Cdd:cd00176   132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
                         170
                  ....*....|....*....
gi 542133174  281 MRHLEGQLEEKNQELQRAR 299
Cdd:cd00176   195 WEELLELAEERQKKLEEAL 213
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
124-315 1.24e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 40.66  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  124 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 199
Cdd:cd07666    14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  200 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 264
Cdd:cd07666    93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 542133174  265 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 315
Cdd:cd07666   170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
T4SS pfam07996
Type IV secretion system proteins; Members of this family are components of the type IV ...
131-244 4.50e-03

Type IV secretion system proteins; Members of this family are components of the type IV secretion system. They mediate intracellular transfer of macromolecules via a mechanism ancestrally related to that of bacterial conjugation machineries.


Pssm-ID: 254572  Cd Length: 195  Bit Score: 38.48  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   131 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME-------ERITTLEKryLSAQREST- 202
Cdd:pfam07996   72 YDLVLDGYGGLSSSAKSLYSKEKLFDTCSYPSGSRASICQRSADKAAQDKAVGEqaydqatNRLSQIEQ--LRSQIDSAk 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 542133174   203 ---SIHDMNDKLENELA--NKEAILRQMEEKNRQLQERLElAEQKLQ 244
Cdd:pfam07996  150 dpkEIADLQARIQAEQAmlQNEQTKLQMLQMLQEAEERLE-EQQAAE 195
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
750-807 4.67e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886  Cd Length: 56  Bit Score: 36.45  E-value: 4.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 542133174  750 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 807
Cdd:cd09487     2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
874-918 5.87e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900  Cd Length: 69  Bit Score: 36.13  E-value: 5.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 542133174  874 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 918
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
874-929 6.67e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 254328  Cd Length: 66  Bit Score: 36.11  E-value: 6.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174   874 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 929
Cdd:pfam07647   11 EWLRSIGLPQYADNFRDQGITgAELLLRLTEEDLK-ALGITSVGHRRKILKKIQRLK 66
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
117-250 9.07e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 252261  Cd Length: 154  Bit Score: 36.84  E-value: 9.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   117 IVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmntKYQRDIREAMAQkedmeerittlekryls 196
Cdd:pfam03938   20 VVDVQKVLQ----ESPAGKAAQKQLEKEFKKLQAELEKKEKELQKELQ---KLQATLSEEARK----------------- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   197 aqrestsihdmndKLENELANKEA-ILRQMEEKNRQLQERLELAEQKLQQTMRKA 250
Cdd:pfam03938   76 -------------AKQKELQQKQQeLQQKQQAAQQELQQKQQELLQPIYDKIDKA 117
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
742-808 7.72e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 53.84  E-value: 7.72e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174    742 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 808
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
952-1023 8.20e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 8.20e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174    952 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1023
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
52-348 3.62e-04

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 259052 [Multi-domain]  Cd Length: 305  Bit Score: 42.38  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    52 LEEELAAANQEIVALREQNVHIQRKMaSSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE----TSQIVELQELLEKQ 127
Cdd:pfam14915    4 LQDEIAMLRLEIDTIKNQNQEKEKKY-FEDIKILKEKNDDLQKTIKLNEETLTKTVFQYSGQlnvlKAENTMLNSKLENE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   128 NYEMAQMKERLAALSSRVGEVEQEAE---TARKDLIKTeemntkYQRDIREAMAQKEDMEERITTLEkrylsaqrestsi 204
Cdd:pfam14915   83 KQNKERLETEVESYRSRLAAAIQDHEqsqTSKRDLELA------FQRARDEWLRLQDKMNFDVSNLK------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   205 hDMNDKLENELANKEAILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEER 280
Cdd:pfam14915  144 -DNNEVLSQQLSKAESKFNSLEIELHHTRDALRektLLLEHVQRDLSQAQCqKKEIEHMYQNEQGKVSKYMGKQESLEER 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174   281 MRHLEGQLEEKNQELQRARQR----EKMNEEHNKRLSDTVDRLLTESnERLQLHLKERMAALEEKNVLIQES 348
Cdd:pfam14915  223 LSQLQSENLLLRQQLDDAQNKgdskEKTVINIQDQFQDILKKLQAES-EKQVLLLEERNKELMKECNHLKER 293
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
36-380 5.31e-19

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 91.70  E-value: 5.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   36 EKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmassegstesehLEGMEPGQKVHEKRLSNGSIDSTDETS 115
Cdd:COG1196   670 KELEEELAELEAQLEKLEEELKSLKNELRSLEDL-------------------LEELRRQLEELERQLEELKRELAALEE 730
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 195
Cdd:COG1196   731 ELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLD 810
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHG 275
Cdd:COG1196   811 ALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELE---ELEAEKEELEDELKELEEEKE 887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  276 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQL-----------HLKERMAALEEKNVL 344
Cdd:COG1196   888 ELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDtletelereieRLEEEIEALGPVNLR 967
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 542133174  345 -IQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 380
Cdd:COG1196   968 aIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELD 1004
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
116-386 1.08e-16

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 84.38  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYl 195
Cdd:COG1196   233 KLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERL- 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  196 saqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 274
Cdd:COG1196   312 -------------EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELf 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  275 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE------SNERLQLHLKERMAALEEKNVLIQES 348
Cdd:COG1196   379 EALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEElkeleaELEELQTELEELNEELEELEEQLEEL 458
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 542133174  349 ETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:COG1196   459 RDRLKELEREL---AELQEELQRLEKELSSLEARLDRL 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-381 6.15e-16

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 6.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 193
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   194 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 273
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   274 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 349
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270
                   ....*....|....*....|....*....|..
gi 542133174   350 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
130-382 1.18e-15

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.91  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  130 EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 209
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  210 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 289
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEEL---EEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  290 EKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL----HDKERL 365
Cdd:COG1196   825 RLEQEIEELEEEIEELEEKLDELEEELEEL-EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELreleSELAEL 903
                         250
                  ....*....|....*..
gi 542133174  366 AEEIEKLRSELDQLKMR 382
Cdd:COG1196   904 KEEIEKLRERLEELEAK 920
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
110-382 1.25e-15

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 80.87  E-value: 1.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   110 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 189
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   190 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 269
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   270 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 348
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270
                   ....*....|....*....|....*....|....
gi 542133174   349 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
112-382 1.47e-15

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.53  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQ-------EAETARKDLIKTEEM----NTKYQRDIREAMAQK 180
Cdd:COG1196   162 EEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKqleklerQAEKAERYQELKAELreleLALLLAKLKELRKEL 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  181 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 260
Cdd:COG1196   242 EELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEEL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  261 AQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 340
Cdd:COG1196   322 EERLEEL---KEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNE 398
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 542133174  341 KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 382
Cdd:COG1196   399 LEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTE 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-328 2.24e-15

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 80.10  E-value: 2.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 100
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   101 ---------KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR 171
Cdd:TIGR02168  780 aeaeieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   172 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT----M 247
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriD 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   248 RKAETLPEV------------------EAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRA 298
Cdd:TIGR02168  940 NLQERLSEEysltleeaealenkieddEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEA 1015
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 542133174   299 RQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 328
Cdd:TIGR02168 1016 KETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
78-381 2.25e-15

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.14  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   78 ASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK 157
Cdd:COG1196   665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  158 DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 237
Cdd:COG1196   745 ELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  238 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErhgNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 317
Cdd:COG1196   825 RLEQEIEELEEEIEELEEKLDELEEELEELEKELE---ELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542133174  318 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErLAEEIEKLRSELDQLKM 381
Cdd:COG1196   902 ELKEE-IEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETE-LEREIERLEEEIEALGP 963
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-380 8.44e-15

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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 78.19  E-value: 8.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    39 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKvHEKrlsngsidstdETSQIV 118
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-EEK-----------LKERLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrdIREAMAQKEDMEERITTLEKRYLSAQ 198
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   199 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH---- 274
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeaql 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   275 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQL--------HLKERMAALEEKNVL-I 345
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvqaelqRVEEEIRALEPVNMLaI 978
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 542133174   346 QESETFRKNLEESLHDKERLAEE---IEKLRSELDQLK 380
Cdd:TIGR02169  979 QEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKK 1016
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
21-318 1.31e-14

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.45  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHE 100
Cdd:COG1196   718 LEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELE----EKRQALQE 793
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  101 KRLS-NGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 179
Cdd:COG1196   794 ELEElEEELEEAER--RLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAE 871
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  180 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAE 259
Cdd:COG1196   872 KEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEE-YEDTLETELERE 950
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174  260 LAQ---RIAAL----TKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDR 318
Cdd:COG1196   951 IERleeEIEALgpvnLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEViEELDKEKRERFKETFDK 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
36-379 1.52e-14

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 77.40  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    36 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEG--STESEHLEGMEPGQKVHEKRLSNGSIDSTDE 113
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqiSALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   114 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdlikteemntkyqRDIREAMAQKEDMEERITTLEKR 193
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--------------EALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   194 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEER 273
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----------ALLNERASLEEALALLRSE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   274 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLkERMAALEEKNVLiqesetfrk 353
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL-EEAEALENKIED--------- 965
                          330       340
                   ....*....|....*....|....*.
gi 542133174   354 nleeslhDKERLAEEIEKLRSELDQL 379
Cdd:TIGR02168  966 -------DEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
135-382 3.56e-14

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 76.25  E-value: 3.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   135 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 214
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   215 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 287
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   288 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMA----------ALEEKNVLIQESETFRKN 354
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASleealallrsELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|..
gi 542133174   355 LEESLHDK----ERLAEEIEKLRSELDQLKMR 382
Cdd:TIGR02168  913 LRRELEELreklAQLELRLEGLEVRIDNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-380 4.67e-14

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 4.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   137 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 216
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   217 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 292
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   293 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 370
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
                          250
                   ....*....|
gi 542133174   371 KLRSELDQLK 380
Cdd:TIGR02168  465 ELREELEEAE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
117-388 4.67e-14

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 4.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   117 IVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 196
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   197 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMRKAETLPEVEAELAQRIAALTK 269
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   270 AEERhgnIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtvdrlLTESNERLQLHLKERMAALEEKNVLIQES 348
Cdd:TIGR02168  839 RLED---LEEQIEELSEDIESLAAEIEELEeLIEELESELEA---------LLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 542133174   349 ETFRKNLEeslHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR02168  907 ESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
116-386 6.90e-14

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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 6.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 195
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   196 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLqqtmrkaETLPEVEAELAQRIAALtkaEERHG 275
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEEL---EEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   276 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 354
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
                          250       260       270
                   ....*....|....*....|....*....|..
gi 542133174   355 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
19-290 1.05e-13

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 74.37  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   19 EVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGM 92
Cdd:COG1196   243 ELEEELSRLEEELEELQEELEEAE----KEIEELKSELEELREELEELQEELLELKEEIEELEGEISllrerlEELENEL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   93 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 172
Cdd:COG1196   319 EELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNE 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  173 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET 252
Cdd:COG1196   399 LEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQR 478
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 542133174  253 LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 290
Cdd:COG1196   479 LEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
19-391 1.87e-13

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 73.64  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   19 EVLKALKSLFEHHKALDEKVRERLRVSLERvsaLEEELAAANQEIVAL------REQNVHIQRKMASSEGSTESEHLEGM 92
Cdd:COG0419   171 KLSELLKEVIKEAKAKIEELEGQLSELLED---IEDLLEALEEELKELkkleeiQEEQEEEELEQEIEALEERLAELEEE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   93 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmntkYQRD 172
Cdd:COG0419   248 KERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEE----LLEK 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  173 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANK----EAILRQMEEKNRQLQERLELAEQKLQQTMR 248
Cdd:COG0419   324 LKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERleelEKELEKALERLKQLEEAIQELKEELAELSA 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  249 K----AETLPEVEAELAQRIAALTKAEERHGNIEERmrhLEGQLEEKNQELQRARQREK-------MNEEHNKRLSDTVD 317
Cdd:COG0419   404 AleeiQEELEELEKELEELERELEELEEEIKKLEEQ---INQLESKELMIAELAGAGEKcpvcgqeLPEEHEKELLELYE 480
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174  318 RLLTESNERLQL--HLKERMAALEEKNVLIQESET-FRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTI 391
Cdd:COG0419   481 LELEELEEELSRekEEAELREEIEELEKELRELEEeLIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQL 557
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-274 1.98e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    31 HKALDEKVRERLRVSlERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLsngsiDS 110
Cdd:TIGR02168  266 EEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE-----EL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   111 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTL 190
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   191 EKRyLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 270
Cdd:TIGR02168  420 QQE-IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497

                   ....
gi 542133174   271 EERH 274
Cdd:TIGR02168  498 QENL 501
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
14-318 2.68e-13

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   14 VSSEVEVLKALKSLFEHHKALDEKVRE-RLRVSLERVSALEEELAAANQEIVALREQnvHIQRKMASSEGSTESEHLEgm 92
Cdd:COG1196   198 LEKQLEKLERQAEKAERYQELKAELRElELALLLAKLKELRKELEELEEELSRLEEE--LEELQEELEEAEKEIEELK-- 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   93 epgQKVHEKRLsngsiDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 172
Cdd:COG1196   274 ---SELEELRE-----ELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  173 IREAMAQKEDMEERITTLE-KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ----ERLELAEQKLQQTM 247
Cdd:COG1196   346 LEELEQLLAELEEAKEELEeKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIEsleeRLERLSERLEDLKE 425
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542133174  248 RKAETLPEVEA---ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDR 318
Cdd:COG1196   426 ELKELEAELEElqtELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
112-440 2.88e-13

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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 73.18  E-value: 2.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEE----MNTKYQRDIREAMAQKEDMEERI 187
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   188 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK------NRQLQ-----------------------ERLEL 238
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeEEQLRvkekigeleaeiaslersiaekeRELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   239 AEQKLQQTM----RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR--------EKMNE 306
Cdd:TIGR02169  320 AEERLAKLEaeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyreklEKLKR 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   307 EHNKrLSDTVDRLLTE----SNERLQLH-----LKERMAALE-EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 376
Cdd:TIGR02169  400 EINE-LKRELDRLQEElqrlSEELADLNaaiagIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   377 DQLKMRTGSLIEPTiprthldtsAELRYSVGSLVDSQSDYR-TTKVIRRPRRGRMGVRRDEPKVK 440
Cdd:TIGR02169  479 DRVEKELSKLQREL---------AEAEAQARASEERVRGGRaVEEVLKASIQGVHGTVAQLGSVG 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
132-386 2.96e-13

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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 73.18  E-value: 2.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   132 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKL 211
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   212 ENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKaETLPEVEAElaqriaaLTKAEERHGNIEERMRHLEGQL 288
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEdlhKLEEALNDLEARLSH-SRIPEIQAE-------LSKLEEEVSRIEARLREIEQKL 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   289 EEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDkerLAEE 368
Cdd:TIGR02169  822 NRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---LKKE 890
                          250
                   ....*....|....*...
gi 542133174   369 IEKLRSELDQLKMRTGSL 386
Cdd:TIGR02169  891 RDELEAQLRELERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-330 4.94e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 72.40  E-value: 4.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    24 LKSLFEHHKALDEKVRE--RLRVSLER-VSALEEELAAANQEIVALREQNVHIQRKMASSegSTESEHLEGMEpgqKVHE 100
Cdd:TIGR02168  234 LEELREELEELQEELKEaeEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYAL--ANEISRLEQQK---QILR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   101 KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYqrdireamaqk 180
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL---EELESRL----------- 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   181 EDMEERITTLEKRYLSAQRESTSIhdmndklENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEA 258
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEE 447
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174   259 ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 330
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
PRK02224 PRK02224
chromosome segregation protein; Provisional
18-435 1.07e-12

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.22  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   18 VEVLKALKSLFEHHkaldEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEpgqk 97
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEERDDLLAEAG---- 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   98 vhekrLSNGSIDSTDE-----TSQIVELQELLEKQ-------NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEm 165
Cdd:PRK02224  304 -----LDDADAEAVEArreelEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEARE- 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  166 ntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqq 245
Cdd:PRK02224  378 ------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA---- 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  246 tMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLT 321
Cdd:PRK02224  448 -LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIA 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  322 ESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSA 400
Cdd:PRK02224  527 ERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIA 602
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 542133174  401 ELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 435
Cdd:PRK02224  603 DAEDEIERLREKREALAE---LNDERRERLAEKRE 634
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-388 1.78e-12

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


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 70.47  E-value: 1.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   112 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 184
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   185 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 264
Cdd:TIGR02168  337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   265 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 342
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 542133174   343 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
PRK03918 PRK03918
chromosome segregation protein; Provisional
12-378 5.68e-12

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.55  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   12 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEG 91
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSE 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   92 MEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT---- 167
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkr 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  168 -------KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN--------------------------E 214
Cdd:PRK03918  381 ltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaE 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  215 LANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQ 287
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGE 540
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  288 LEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESETFRK---NLEESLHDKER 364
Cdd:PRK03918  541 IKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELER 616
                         410
                  ....*....|....
gi 542133174  365 LAEEIEKLRSELDQ 378
Cdd:PRK03918  617 EEKELKKLEEELDK 630
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
113-388 1.12e-11

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 67.86  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  113 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK--EDMEERITTL 190
Cdd:COG0419   165 GLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQeiEALEERLAEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  191 EKRYLSAQRESTSIHDMN-------DKLENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKAETLPEVEAEL 260
Cdd:COG0419   245 EEEKERLEELKARLLEIEslelealKIREEELRELERLLEELEEKIERLEElerEIEELEEELEGLRALLEELEELLEKL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  261 AQRIAALTKAEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLL------TESNERLQLHLKER 334
Cdd:COG0419   325 KSLEERLEKLEEKLEKLESELEELA---EEKNELAKLLEERLKELEERLEELEKELEKALerlkqlEEAIQELKEELAEL 401
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 542133174  335 MAALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG0419   402 SAALEEIQEELEELEKELEELEREL---EELEEEIKKLEEQINQLESKELMIAE 452
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
14-388 1.47e-11

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 67.48  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   14 VSSEVEVLKALKSLFEHHKALDEKVRERLRvslERVSALEEELAAANQEIVALRE--QNVHIQRKMASSEGSTESEHLEG 91
Cdd:COG0419   331 LEKLEEKLEKLESELEELAEEKNELAKLLE---ERLKELEERLEELEKELEKALErlKQLEEAIQELKEELAELSAALEE 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   92 MEPGQKVHEKRLSngsiDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG-------EVEQEAETARKDLIKTEE 164
Cdd:COG0419   408 IQEELEELEKELE----ELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcgqELPEEHEKELLELYELEL 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  165 MNTKYQRDIREamaQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENEL-ANKEAILRQMEE----KNRQLQERLELA 239
Cdd:COG0419   484 EELEEELSREK---EEAELREEIEELEKELRELEEELIELLELEEALKEELeEKLEKLENLLEEleelKEKLQLQQLKEE 560
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  240 EQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN--KRLSDTVD 317
Cdd:COG0419   561 LRQLEDRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEaeEELESELE 640
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542133174  318 RL-----LTESNERLQLHLKERMAALEEK-NVLIQESETfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:COG0419   641 KLnlqaeLEELLQAALEELEEKVEELEAEiRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQ 716
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
16-307 1.61e-11

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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 67.40  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    16 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES-------- 86
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersiaek 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    87 -EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteem 165
Cdd:TIGR02169  314 eRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL------ 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   166 nTKYQRDIREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQ 245
Cdd:TIGR02169  388 -KDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174   246 TmrkaetlpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 307
Cdd:TIGR02169  460 L-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
3-379 2.33e-11

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 66.71  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    3 VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVhiQRKMASSEG 82
Cdd:COG0419   247 EKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLE--ELEELLEKL 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   83 STESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT 162
Cdd:COG0419   325 KSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAA 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  163 EEmntKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQM-----EEKNRQLQERLE 237
Cdd:COG0419   405 LE---EIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIA-ELAGAGEKCPVCgqelpEEHEKELLELYE 480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  238 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnKRLSDTVD 317
Cdd:COG0419   481 LELEELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKE--KLQLQQLK 558
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133174  318 RLLTESNERLQlHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:COG0419   559 EELRQLEDRLQ-ELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSL 619
PRK03918 PRK03918
chromosome segregation protein; Provisional
135-386 4.27e-11

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.86  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  135 KERLAALSSRVGEVEQEAETARKDLIKTEemntkyqRDIREAMAQKEDMEERITTLEKRYlsaqRESTSIHDMNDKLENE 214
Cdd:PRK03918  178 IERLEKFIKRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKLEKEV----KELEELKEEIEELEKE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  215 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE--AELAQRIAAL-TKAEERHGNIEERMRHLEGQLEEK 291
Cdd:PRK03918  247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  292 NQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQ--LHLKERMAALEEKnVLIQESETFRKNLEESLHDKERLAE 367
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEeaKAKKEELERLKKR-LTGLTPEKLEKELEELEKAKEEIEE 405
                         250
                  ....*....|....*....
gi 542133174  368 EIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918  406 EISKITARIGELKKEIKEL 424
mukB PRK04863
cell division protein MukB; Provisional
39-386 8.23e-11

cell division protein MukB; Provisional


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 64.98  E-value: 8.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   39 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 115
Cdd:PRK04863  278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 193
Cdd:PRK04863  356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  194 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 272
Cdd:PRK04863  415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  273 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 350
Cdd:PRK04863  494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 542133174  351 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK04863  566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
14-381 3.67e-10

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 62.86  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   14 VSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQR-KMASSEGSTESEHLEGM 92
Cdd:COG0419   377 LEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEqINQLESKELMIAELAGA 456
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   93 E--------PGQKVHEKRLS----------NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSS-RVGEVEQEAE 153
Cdd:COG0419   457 GekcpvcgqELPEEHEKELLelyeleleelEEELSREKEEAELREEIEELEKELRELEEELIELLELEEaLKEELEEKLE 536
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  154 TARKDLIKTEEMNTKYQR-DIREAMAQKEDMEERITTLEKRYLsaqrestsihdmndkLENELANKEAILRQMEEKNRQL 232
Cdd:COG0419   537 KLENLLEELEELKEKLQLqQLKEELRQLEDRLQELKELLEELR---------------LLRTRKEELEELRERLKELKKK 601
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  233 QERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAEERHG-------NIEERMRHLEGQLEEKNQELQRARQREKMN 305
Cdd:COG0419   602 LKELEERLSQLEELLQSLELS-EAENELEEAEEELESELEKLNlqaeleeLLQAALEELEEKVEELEAEIRRELQRIENE 680
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133174  306 EEHNKRLSDTvdrlltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 381
Cdd:COG0419   681 EQLEEKLEEL---------EQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALELLEE 747
PTZ00121 PTZ00121
MAEBL; Provisional
32-361 4.33e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   32 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRlsngsidST 111
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKK-------KA 1548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLE 191
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  192 KRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQ 262
Cdd:PTZ00121 1625 LK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAK 1702
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  263 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
                         330       340
                  ....*....|....*....|..
gi 542133174  340 EKnvLIQESETFRKNLEESLHD 361
Cdd:PTZ00121 1783 EE--LDEEDEKRRMEVDKKIKD 1802
PRK03918 PRK03918
chromosome segregation protein; Provisional
47-386 4.36e-10

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   47 ERVSALEEELAAANQEIVALREQnvhiQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDstdetSQIVELQELLEK 126
Cdd:PRK03918  193 ELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKEEIEELEKELESLE-----GSKRKLEEKIRE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  127 QNYEMAQMKERLAALSSRVGEVEqEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHD 206
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  207 MNDKLEnELANKEAILRQME---EKNRQLQERLELAEQKLqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRH 283
Cdd:PRK03918  343 LKKKLK-ELEKRLEELEERHelyEEAKAKKEELERLKKRL-----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  284 LEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDRLLTESNERLQ-LHLKERMAALEEKNV---LIQESETF 351
Cdd:PRK03918  417 LKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKeIEEKERKLRKELRELekvLKKESELI 496
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 542133174  352 R--------KNLEESL--HDKERL---AEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918  497 KlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKGEIKSL 544
PRK02224 PRK02224
chromosome segregation protein; Provisional
47-386 1.20e-09

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.21  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   47 ERVSALEEELAAANQEIV-ALREQNVHIQRKMASSEGSTES-----EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVEL 120
Cdd:PRK02224  310 EAVEARREELEDRDEELRdRLEECRVAAQAHNEEAESLREDaddleERAEELREEAAELESELEEAREAVEDRREEIEEL 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  121 QELLE--------------KQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----RDIREA--MAQ 179
Cdd:PRK02224  390 EEEIEelrerfgdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSphVET 469
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  180 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PE 255
Cdd:PRK02224  470 IEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAE 548
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  256 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQR-ARQREKMNEEHNKRlsDTVDRL------LTESNERLQ 328
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAE--DEIERLrekreaLAELNDERR 626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  329 LHLKERM------------AALEEKNVLIQESETFRKNLEESLHDK--------------ERLAEEIEKLRSELDQLKMR 382
Cdd:PRK02224  627 ERLAEKRerkreleaefdeARIEEAREDKERAEEYLEQVEEKLDELreerddlqaeigavENELEELEELRERREALENR 706

                  ....
gi 542133174  383 TGSL 386
Cdd:PRK02224  707 VEAL 710
PRK03918 PRK03918
chromosome segregation protein; Provisional
13-382 1.61e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   13 GVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEG 91
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKA 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   92 MEPGQKVHEKRLSNGSIDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETA 155
Cdd:PRK03918  370 KKEELERLKKRLTGLTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEH 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  156 RKDLIK--TEEMNtKYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ- 231
Cdd:PRK03918  450 RKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEy 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  232 --LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMN 305
Cdd:PRK03918  528 ekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFY 601
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  306 EEHNkRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRS 374
Cdd:PRK03918  602 NEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRA 680

                  ....*...
gi 542133174  375 ELDQLKMR 382
Cdd:PRK03918  681 ELEELEKR 688
PTZ00121 PTZ00121
MAEBL; Provisional
32-388 1.71e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   32 KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDST 111
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  112 DETSQIVE---LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQK 180
Cdd:PTZ00121 1493 EEAKKKADeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAK 1570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  181 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAE 251
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAE 1650
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  252 TLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHL 331
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAE 1725
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  332 KERMAALEEknvLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:PTZ00121 1726 EENKIKAEE---AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
24-380 1.77e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 60.86  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    24 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEpgqKVHEKRL 103
Cdd:pfam12128  329 LELLEDQKGAFEDADIEQLQADLDQLPSIRSELEEVEARLDALTGKHQDVQRKYERLKQKIKEQLERDLE---KNNERLA 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   104 SngSIDSTDETSQIVE--LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKE 181
Cdd:pfam12128  406 A--IREEKDRQKAAIEedLQALESQLRQQLEAGKLEFNEEEYELELRLGRLKQRLDSATATPEELE----QLEINDEALE 479
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   182 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK------------ 249
Cdd:pfam12128  480 KAQEEQEQAEANVEQLQSELRQLRKRRDEALEALQRAERRLLQLRQALDELELQLSPQAGSLLHFLRNeapgweesigkv 559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   250 --AETL------PEV---------------------------EAELAQRIAALTK----AEERHGNIEERMRHLEGQLEE 290
Cdd:pfam12128  560 isPELLertdldPQLvegsdsdtlygvsldlqrldvpdyaanETELRERLQQAEEalqsAVAKQKQAEEQLVQANAELEE 639
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   291 KNQELQRARQREKMNEEHNKRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD----- 361
Cdd:pfam12128  640 QKRAEAEARTALKQARLDLQRLQNEQQSLKDKLElaiaERKQQAETQLRQLDAQLKQLLEQQQAFLEALKDDFRElrter 719
                          410
                   ....*....|....*....
gi 542133174   362 KERLAEEIEKLRSELDQLK 380
Cdd:pfam12128  720 LAKWQVVEGELDNQLAQLS 738
RecN COG0497
ATPase involved in DNA repair [DNA replication, recombination, and repair]
119-301 1.86e-09

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223571 [Multi-domain]  Cd Length: 557  Bit Score: 60.31  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  119 ELQELLEKQNyEMAQMKERLA-------ALSSRVGEVEQEAETaRKDLIKTEEMNTKYQrDIREAMAQKEDM---EERIT 188
Cdd:COG0497   172 ELEDLQEKER-ERAQRADLLQfqleeleELNLQPGEDEELEEE-RKRLSNSEKLAEAIQ-NALELLSGEDDTvsaLSLLG 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  189 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQQTM---RK----AETLPEVEA 258
Cdd:COG0497   249 RALEALEDLSEYDGKLSELAELLEEALYELEEASEELRAYLDELEfdpNRLEEVEERLFALKslaRKygvtIEDLLEYLD 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 542133174  259 ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 301
Cdd:COG0497   329 KIKEELAQLDNSEESLEALEKEVKKLKAELLEAAEALSAIRKK 371
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
122-403 1.91e-09

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


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   122 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 196
Cdd:TIGR02168  203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   197 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 276
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   277 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 356
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 542133174   357 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 403
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
PRK03918 PRK03918
chromosome segregation protein; Provisional
138-386 2.43e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  138 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 215
Cdd:PRK03918  127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  216 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 292
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  293 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 364
Cdd:PRK03918  283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
                         250       260
                  ....*....|....*....|..
gi 542133174  365 LAEEIEKLRSELDQLKMRTGSL 386
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGL 384
PRK03918 PRK03918
chromosome segregation protein; Provisional
112-357 2.85e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  112 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIREAMAQKEDMEERIT 188
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKIR 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  189 TLEKRylsaqrestsIHDMNDKLEnELANKEAILRQMEEKN---RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 265
Cdd:PRK03918  263 ELEER----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  266 ALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLS----DTVDRLLTESNERLQLHLKERMAAL 338
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKIT 411
                         250
                  ....*....|....*....
gi 542133174  339 EEKNVLIQESETFRKNLEE 357
Cdd:PRK03918  412 ARIGELKKEIKELKKAIEE 430
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
198-386 3.20e-09

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.73  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  198 QRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 277
Cdd:COG1196   659 KRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQ---L 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  278 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------LTESNERLQLHLKERMAALEEKNVLIQESETF 351
Cdd:COG1196   736 QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLkeeieeLEEKRQALQEELEELEEELEEAERRLDALERE 815
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 542133174  352 RKNLEESLHDK----ERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:COG1196   816 LESLEQRRERLeqeiEELEEEIEELEEKLDELEEELEEL 854
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
21-386 3.58e-09

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 253253 [Multi-domain]  Cd Length: 722  Bit Score: 59.56  E-value: 3.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    21 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIValreQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 100
Cdd:pfam05557  187 LKLLESELEELREQLEECQKELAEAEKKLQSLTSEQASSADNSV----KIKHLEEELKRYEQDAEVVKSMKEQLLQIPEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   101 KRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQK 180
Cdd:pfam05557  263 ERELAALREENRKLRSMKEDNELLKEELEDLQSRLERFEKMREKLADLELEKEKLENELKSWKSLLQ----DIGLNLRTP 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   181 EDMEERITTLEKRYLSAQRESTSIhdmndklenelankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 260
Cdd:pfam05557  339 DDLSRRIVVLQNEELQLKEKNGSI--------------SSSAKQLETTLQQLQLERQKAVSEILELKKKLEALKALVRRL 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   261 AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN---EEHNKRLSDTVDRLLTESNERLQLHLKERMAA 337
Cdd:pfam05557  405 QRRLTLVTKERDGLRAILNSYDKELTETSVSGQLMKRLEEAEDLVqkvQSHLAKMENQLSELEEDVGQQKDRNNTLETEI 484
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 542133174   338 --LEEKNVLIQESETFRKNLEESLHDK-ERLAEEIEKLRSELDQLKMRTGSL 386
Cdd:pfam05557  485 klLKEQLVSNERLLSFVKEATNALRLKiETLERERDRLRQEKSLLEMKLEHL 536
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
118-379 7.34e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 58.55  E-value: 7.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   118 VELQELLEKQnyeMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ-KEDMEERITTL--EKRY 194
Cdd:pfam12128  620 VAKQKQAEEQ---LVQANAELEEQKRAEAEARTALKQARLDLQRLQNEQQSLKDKLELAIAErKQQAETQLRQLdaQLKQ 696
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   195 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKlqQTMRKAEtLPEVEAELAQRIAALtkaeerh 274
Cdd:pfam12128  697 LLEQQQAFLEALKDDFRELRTERLAKWQVVEGELDNQLAQLSAAIEAA--RTQAKAR-LKELKKQYDRELASL------- 766
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   275 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQLHLKERMAALEE----KNVLIQES 348
Cdd:pfam12128  767 DVDPNTVKELKRQIEELETTIERIAVRRPEVREYRAFMQETWLHRdsLREERPNLAIQLRELESSAEElqqeLTRLIKDT 846
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 542133174   349 ETFRKNLEESLHDKE----RLAEEIEKLRSELDQL 379
Cdd:pfam12128  847 KLRRKKLEQERKALEkqldQLDELLRGLRDEMRQL 881
COG4372 COG4372
Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]
116-319 1.26e-08

Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 57.34  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMN-------TKYQRDIREAMAQKEDMEERIT 188
Cdd:COG4372    75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELaaarqnlAKAQQELARLTKQAQDLQTRLK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  189 TL--EKRYLSAQREStsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 266
Cdd:COG4372   155 TLaeQRRQLEAQAQS---------LQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARRAAA 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 542133174  267 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 319
Cdd:COG4372   226 AQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQL 278
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
5-544 1.29e-08

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    5 KRQAQSPSGVSSEVEVLKA-LKSLFEHHKALDEKVRERLRvslERVSALEEELAAANQEIVALREQNVHIQRKMASSEGS 83
Cdd:COG1196   336 KEELEERETLLEELEQLLAeLEEAKEELEEKLSALLEELE---ELFEALREELAELEAELAEIRNELEELKREIESLEER 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   84 TESEHLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIK 161
Cdd:COG1196   413 LERLSERLEDLKEELKELEAELEELQTELEElnEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDR 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  162 TEEMNTKYQRDIREAMAQKEDMEERITTL------EKRYLSA-------------------------------------- 197
Cdd:COG1196   493 LEAEQRASQGVRAVLEALESGLPGVYGPVaelikvKEKYETAleaalgnrlqavvveneevakkaieflkenkagratfl 572
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  198 ------QRESTSIHDMNDKLEN----------------------------ELANKEAILRQME----------------- 226
Cdd:COG1196   573 pldrikPLRSLKSDAAPGFLGLasdlidfdpkyepavrfvlgdtlvvddlEQARRLARKLRIKyrivtldgdlvepsgsi 652
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  227 -----EKNRQLQERLELA--EQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR 299
Cdd:COG1196   653 tggsrNKRSSLAQKRELKelEEELAELEAQLE---KLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALE 729
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  300 QREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALEEKNVLIQESETFRKN-LEESLHDKERLAEEIEKLRSELDQ 378
Cdd:COG1196   730 EELEQLQSRLEELEEELEELEEELEE-----LQERLEELEEELESLEEALAKLKEeIEELEEKRQALQEELEELEEELEE 804
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  379 LKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKvkslgdhewNRTQQIGVLSS 458
Cdd:COG1196   805 AERRLDAL------------ERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE---------ELEKELEELKE 863
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  459 HPFESDTEMSDIDDDdretifssmdllspsgHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 538
Cdd:COG1196   864 ELEELEAEKEELEDE----------------LKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVE 927

                  ....*.
gi 542133174  539 GLNLAR 544
Cdd:COG1196   928 LPELEE 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
167-380 1.46e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   167 TKYQRDIREAMAQKEDMEERITTLE---------KRYLSAQRESTSI-HDMNDKLENelANKEAILRQMEEKNRQLqERL 236
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEKAERyKELKAELRE--LELALLVLRLEELREEL-EEL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   237 ELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 315
Cdd:TIGR02168  245 QEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133174   316 VDRL----------LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 380
Cdd:TIGR02168  325 LEELeskldelaeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
40-388 2.26e-08

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: 56.90  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    40 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 119
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   120 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 199
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   200 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 273
Cdd:TIGR00618  353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   274 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 334
Cdd:TIGR00618  430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 542133174   335 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 388
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
36-361 3.34e-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: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 56.62  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    36 EKVRERL---RVSLERVSALEEELaaaNQEIVALREQNVHIQRKMASSEgstESEHLEGMEPGQKV--HEKRLSNGSIDS 110
Cdd:TIGR02169  173 EKALEELeevEENIERLDLIIDEK---RQQLERLRREREKAERYQALLK---EKREYEGYELLKEKeaLERQKEAIERQL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   111 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEV-EQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 189
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   190 LEKRYLSAQRE----STSIHDMN---DKLENELANKEAIL--------------------------------RQMEEKNR 230
Cdd:TIGR02169  327 LEAEIDKLLAEieelEREIEEERkrrDKLTEEYAELKEELedlraeleevdkefaetrdelkdyrekleklkREINELKR 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   231 QLQerlelaeqklqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 310
Cdd:TIGR02169  407 ELD--------------RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 542133174   311 RLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD 361
Cdd:TIGR02169  473 DLKEEYDRV-----EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
41-379 4.10e-08

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: 56.13  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174    41 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDET 114
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   115 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 194
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   195 LSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 269
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   270 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 339
Cdd:TIGR00618  759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 542133174   340 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 379
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
PRK03918 PRK03918
chromosome segregation protein; Provisional
116-376 4.88e-08

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  116 QIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIREAMAQKEDMEERITTLEKRY 194
Cdd:PRK03918  504 QLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKEL 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  195 LSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQRIA 265
Cdd:PRK03918  580 EELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELE 650
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  266 ALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLSDTVDRLLTEsnerlqlhLKERMAALEEKnv 343
Cdd:PRK03918  651 ELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEK--------LKEELEEREKA-- 709
                         250       260       270
                  ....*....|....*....|....*....|...
gi 542133174  344 lIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 376
Cdd:PRK03918  710 -KKELE----KLEKALERVEELREKVKKYKALL 737
PRK02224 PRK02224
chromosome segregation protein; Provisional
197-384 5.64e-08

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  197 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 276
Cdd:PRK02224  197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174  277 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 340
Cdd:PRK02224  277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 542133174  341 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 384
Cdd:PRK02224  357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
DNA_S_dndD TIGR03185
DNA sulfur modification protein DndD; This model describes the DndB protein encoded by an ...
120-377 5.72e-08

DNA sulfur modification protein DndD; This model describes the DndB protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndD is described as a putative ATPase. The small number of examples known so far include species from among the Firmicutes, Actinomycetes, Proteobacteria, and Cyanobacteria [DNA metabolism, Restriction/modification].


Pssm-ID: 234141 [Multi-domain]  Cd Length: 650  Bit Score: 55.46  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   120 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA----MAQKEDMEERITTLEKRYL 195
Cdd:TIGR03185  200 KSELPSSILSEIEALEAELKEQSEKYEDLAQEIAHLRNELEEAQRSLESLEKKFRSEggdlFEEREQLERQLKEIEAARK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   196 SAQRESTS----------IHDMNDKLENELANKEAILRqmeekNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 265
Cdd:TIGR03185  280 ANRAQLRElaadplplllIPNLLDSTKAQLQKEEQSQQ-----NQLTQEELEERDKELLESLPKLALPAEHVKEIAAELA 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   266 ALTKAEERHGNIEERMRHLE-GQLEEKNQELQRARQREKMN----EEHNKRLSDTVDRLLTE--SNERLQlHLKErmaAL 338
Cdd:TIGR03185  355 EIDKPATTDSEIPHRLSGSElTQLEVLIQQVKRELQDAKSQllkeLRELEEELAEVDKKISTipSEEQIA-QLLE---EL 430
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 542133174   339 EEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELD 377
Cdd:TIGR03185  431 GEAQNELFRSEAEIEELLRQL---ETLKEAIEALRKTLD 466
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
119-373 6.32e-08

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: 55.82  E-value: 6.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   119 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQkEDMEERITTLEKRYLSAQ 198
Cdd:TIGR00606  574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSS 652
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   199 RESTSIH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA----QRIAALTKA 270
Cdd:TIGR00606  653 KQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLA 732
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133174   271 EERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHLKERMAALEEK 341
Cdd:TIGR00606  733 PGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDVERKIAQQ 811
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 542133174   342 NVLIQESE------TFRKNLEESLHDKERLAEEIEKLR 373
Cdd:TIGR00606  812 AAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
32-382 1.04e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended