|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
138-452 |
2.31e-140 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 407.38 E-value: 2.31e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 138 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQsQNTGVARsLEPFFENYLSTLRRQLDTKQSERGRLDMELR 217
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 218 NVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVIL 297
Cdd:pfam00038 79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 298 SMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKK 377
Cdd:pfam00038 159 EMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22164776 378 QCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:pfam00038 239 QKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
62-135 |
2.16e-27 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 107.82 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 62 LYNLGG-KNISVSMA-----------CGASSGRALG-------------------GFGSGAYVGLGASRQTFG------- 103
Cdd:pfam16208 45 LYNLGGsKSISISVAgggsrpgsgfgFGGGGGGGFGggfgggggggfgggggfggGFGGGGYGGGGFGGGGFGgrggfgg 124
|
90 100 110
....*....|....*....|....*....|..
gi 22164776 104 PVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRV 135
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-454 |
2.23e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 130 PEIQRVRtqerEQIKTLNNKFASFIDKVRflEQQNKVLETKwALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSER 209
Cdd:TIGR02169 674 AELQRLR----ERLEGLKRELSSLQSELR--RIENRLDELS-QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 210 GRLDMELRNVQDNLEDfknkYEDEINkrtALENEFVLLKKDVDAAYmgRMDLHGKVDSLTQEIDFLqqlfEMELSQVQTN 289
Cdd:TIGR02169 747 SSLEQEIENVKSELKE----LEARIE---ELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKL----EEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 290 VSDTNVILSMDNNRNLDLDSIIAEVKAQYELIA--QKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQR 367
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 368 LQGEVDAAKKQCQQLQTAIAEAEQNgemalkdakkkLGDLDTALHQAKEDLARMLREYQDLVSVKlALDMEIATYRKLLE 447
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKR-----------LSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQ 961
|
....*..
gi 22164776 448 SEESRMS 454
Cdd:TIGR02169 962 RVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-434 |
1.82e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 88 GSGAYVGlGASRQTFGPVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRVRTQERE---QIKTLNNKFASFIDKVRFLEQQN 164
Cdd:TIGR02168 657 PGGVITG-GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 165 KVLETKWALLQEQSQNTGVARSLepfFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEF 244
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 245 VLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEmelsqvQTNVSDTNVILSMdNNRNLDLDSIIAEVKAQYELIAQK 324
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIE------ELSEDIESLAAEI-EELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 325 SRAEAESwyQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEaeqNGEMALKDAKKKL 404
Cdd:TIGR02168 886 EEALALL--RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALE 960
|
330 340 350
....*....|....*....|....*....|
gi 22164776 405 GDLDTALHQAKEDLARMLREYQDLVSVKLA 434
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-425 |
4.10e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 158 RFLEQQNKVLETKWALLqeqsqntgvARSLEpFFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFknkyEDEINKr 237
Cdd:TIGR02168 214 RYKELKAELRELELALL---------VLRLE-ELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSE- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 238 taLENEFVLLKKDVDAAYmgrmdlhGKVDSLTQEIDFLQQlfemELSQVQTNVSDTNVILSMDNNRNLDLDSIIAEVKAQ 317
Cdd:TIGR02168 279 --LEEEIEELQKELYALA-------NEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 318 YELIAQK--SRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNG-- 393
Cdd:TIGR02168 346 LEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIee 425
|
250 260 270
....*....|....*....|....*....|....*...
gi 22164776 394 ------EMALKDAKKKLGDLDTALHQAKEDLARMLREY 425
Cdd:TIGR02168 426 llkkleEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
125-404 |
9.33e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 125 NVEIDPEIQrvrtQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNtgvarslepfFENYLSTLRRQLDT 204
Cdd:TIGR04523 358 NSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ----------KDEQIKKLQQEKEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 205 KQSERGRL-----------------DMELRNVQDNLEDFKNK-------YEDEINK-RTALEN---EFVLLKKDVDAAYM 256
Cdd:TIGR04523 424 LEKEIERLketiiknnseikdltnqDSVKELIIKNLDNTRESletqlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 257 GRMDLHGKVDSLTQEIDFL---QQLFEMELSQVQTNVSDTNV-ILSMDNNRNldldsiiaevKAQYELIAQKSRAEAESW 332
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLkekIEKLESEKKEKESKISDLEDeLNKDDFELK----------KENLEKEIDEKNKEIEEL 573
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22164776 333 YQT------KYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIaeaeqngeMALKDAKKKL 404
Cdd:TIGR04523 574 KQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII--------KNIKSKKNKL 643
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-452 |
1.27e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 354 TKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNgemaLKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKL 433
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90
....*....|....*....
gi 22164776 434 ALDMEIATYRKLLESEESR 452
Cdd:TIGR02168 751 QLSKELTELEAEIEELEER 769
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-426 |
2.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 199 RRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYmgrmdLHGKVDSLTQEIdflqql 278
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAEL------ 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 279 femelsqvqtnvsdtnvilsmdnnRNLDLDSiiAEVKaqyELIAQKSRAEAEswyqtkyeelqvtagkhgdsLRDTKNEI 358
Cdd:COG4913 678 ------------------------ERLDASS--DDLA---ALEEQLEELEAE--------------------LEELEEEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 359 AELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNGEMAL---------------------KDAKKKLGDLDTALHQAKED 417
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdaverelrENLEERIDALRARLNRAEEE 788
|
....*....
gi 22164776 418 LARMLREYQ 426
Cdd:COG4913 789 LERAMRAFN 797
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-448 |
3.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 201 QLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQlfe 280
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 281 mELSQVQTNVSDTNVILSMDNNRN-LDLdsiiaevkaqyeLIAQKSRAEAE---SWYQTKYEELQvtagKHGDSLRDTKN 356
Cdd:COG4942 98 -ELEAQKEELAELLRALYRLGRQPpLAL------------LLSPEDFLDAVrrlQYLKYLAPARR----EQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 357 EIAELTRttqrlqgEVDAAKKQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALD 436
Cdd:COG4942 161 ELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|..
gi 22164776 437 MEIATYRKLLES 448
Cdd:COG4942 234 AEAAAAAERTPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
227-450 |
1.27e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 227 KNKYEDEINKRTALENEFVLLKKDVDAAYmgrMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVILSMDNNRNLD 306
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKI---RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 307 LDSIIAEvkaqYELIAQKsraeaeswYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQ----------------- 369
Cdd:pfam15921 669 LNSLSED----YEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqkqi 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 370 ----GEVDAAKKQCQQLQTAIAEAEQNGEMaLKDAKKKLGDLDTALHQAKEDLA---RMLREYQDLVSVKLAlDMEIATY 442
Cdd:pfam15921 737 takrGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVA-NMEVALD 814
|
....*...
gi 22164776 443 RKLLESEE 450
Cdd:pfam15921 815 KASLQFAE 822
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-452 |
1.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 307 LDSIIAEVKAQYE-LIAQKSRAEAESW-YQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQT 384
Cdd:COG1196 244 LEAELEELEAELEeLEAELAELEAELEeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22164776 385 AIAEAEQNGEMA---LKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:COG1196 324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
208-424 |
1.76e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 208 ERGRLDMELRNVQDNLEDFKNKYEDEINKRTALE----------------NEFVLLK-------KDVDAAYMGRMDLHGK 264
Cdd:pfam15905 88 ERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSasvaslekqlleltrvNELLKAKfsedgtqKKMSSLSMELMKLRNK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 265 VDSLTQEIDFLQQLFEMELSQVQTNVSDTNVILSMDNNRNLDLDSIIAEVKAQYE-LIAQKSRAEAESWYQTKYEE---- 339
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEkLLEYITELSCVSEQVEKYKLdiaq 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 340 LQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAakkQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLA 419
Cdd:pfam15905 248 LEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE---KCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQ 324
|
....*
gi 22164776 420 RMLRE 424
Cdd:pfam15905 325 KLQQK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
155-407 |
2.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 155 DKVRFLEQQNKVLETKWALLQEQSQntgvarslepFFENYLSTLRRQLDTKQSergrldmELRNVQDNLEDFKNKYEDEI 234
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK----------TYNKNIEEQRKKNGENIA-------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 235 NKRTALENEFVLLKKDVDAAY----MGRMDLHGKVDSLTQEIDFLQQlfEMELSQVQTNVSDTNVILSmdnnrnlDLDSI 310
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRIT-------KIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 311 IAEVKAQYELIaqksraeaeswyQTKYEELQVTAGKHGD---SLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQ---- 383
Cdd:PHA02562 308 LKELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQaefv 375
|
250 260
....*....|....*....|....*..
gi 22164776 384 ---TAIAEAEQNgemaLKDAKKKLGDL 407
Cdd:PHA02562 376 dnaEELAKLQDE----LDKIVKTKSEL 398
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
326-391 |
2.71e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p 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 Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.44 E-value: 2.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22164776 326 RAEAESWyQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQ 391
Cdd:pfam12718 6 KLEAENA-QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEK 70
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-442 |
2.96e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 131 EIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNtgvarslepffenylstLRRQLDTKQSERG 210
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-----------------LEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 211 RLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAymgrmdLHGKVDSLTQEIDFLQQLFEmELSQVQTNV 290
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLE-ALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 291 SDTNVILSMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESwyQTKYEELQvtagkhgDSLRDTKNEIAELTRTTQRLQG 370
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAA-------EEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22164776 371 EVDAAKKQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARML-REYQDLVSVKLALDMEIATY 442
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAYEAALEAA 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
349-426 |
3.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22164776 349 DSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQngemALKDAKKKLGDLDTALHQAKEDLARMLREYQ 426
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREELGERARALY 96
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
160-452 |
4.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 160 LEQQNKVLETKWALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTA 239
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 240 LENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFE-------------------MELSQVQTNVSDTNVILSMD 300
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAaleqelqalseaeaeqaldELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 301 NNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQ 380
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22164776 381 QLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
302-444 |
6.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 302 NRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQT--KYEELQVTAGKHGDSLRDTKNEIAELTRTT---------QRLQG 370
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEE 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22164776 371 EVDAAKKQCQQLQTAIAEAEQngEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRK 444
Cdd:COG4717 440 ELEELEEELEELREELAELEA--ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-453 |
7.36e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 303 RNLDLDSIIAEVKAQYELIAQKSRAEAEswYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQL 382
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22164776 383 QTAIAEAEQNGEMALKDAKKKLGDLDTALHQ---AKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRM 453
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
312-425 |
7.67e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 312 AEVKAQYELIAQKSRAEAEswYQTKYEELQ----------VTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQ 381
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKE--LRERRNELQklekrllqkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 22164776 382 LQT-AIAEAEQNGEMALKDAKKKLgdLDTALHQAKEDLARMLREY 425
Cdd:PRK12704 136 LIEeQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLIKEI 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-454 |
8.78e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 311 IAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGK--HGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAE 388
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22164776 389 AE---QNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRMS 454
Cdd:COG1196 349 AEeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-277 |
9.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 112 QEVTVNQSLLTPLNVEIDpeiQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNTGVARsLEPFf 191
Cdd:COG4913 269 ERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-LEQL- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 192 ENYLSTLRRQLDTKQSERGRLDMELRNVQ----DNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDS 267
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
170
....*....|
gi 22164776 268 LTQEIDFLQQ 277
Cdd:COG4913 424 LEAEIASLER 433
|
|
| |
