|
Name |
Accession |
Description |
Interval |
E-value |
| PH_RIP |
cd01236 |
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ... |
16-151 |
9.29e-80 |
|
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269942 Cd Length: 136 Bit Score: 258.91 E-value: 9.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 16 IFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQ 95
Cdd:cd01236 1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 96 GTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRT 151
Cdd:cd01236 81 GSIDMSQCTEVTDAEARTGHPHSLAITTPERIHFVKADSKEEIRWWLELLAVYPRT 136
|
|
| PH_M-RIP |
cd13275 |
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ... |
389-467 |
6.32e-26 |
|
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270094 Cd Length: 104 Bit Score: 103.95 E-value: 6.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 389 KKGWLTKQ---------------------YEDGQAAD---LDGEINLSTCYDVTEYPVQRNYGFQIHTKEGE-FTLSAMT 443
Cdd:cd13275 1 KKGWLMKQgsrqgewskhwfvlrgaalkyYRDPSAEEageLDGVIDLSSCTEVTELPVSRNYGFQVKTWDGKvYVLSAMT 80
|
90 100
....*....|....*....|....
gi 1907081936 444 SGIRRNWIQTIMKHVLPASAPDVT 467
Cdd:cd13275 81 SGIRTNWIQALRKAAGLPSPPALP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
655-969 |
1.12e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEAS------DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATspsgawQRLHRVNQDLQSELEAQCRR 728
Cdd:COG1196 198 LERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEEL------EAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 729 QEL----ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQgkvrEQLEEWQHSKA 804
Cdd:COG1196 272 LRLeleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 805 MLSGQLRASEQKLRSTEARLLEKTQELrdLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytlll 884
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL------ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 885 escEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 964
Cdd:COG1196 420 ---EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....*
gi 1907081936 965 RDLIK 969
Cdd:COG1196 497 LEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
709-1068 |
1.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNqDLQSELEAQcrRQELITQQIQTLKhsYGEAKDAIRHHEAEIQTLQTRlgNAAAELAIKEQALAKLKGELKME 788
Cdd:COG1196 186 ENLERLE-DILGELERQ--LEPLERQAEKAER--YRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 789 QGKVREQLEEWQHSKAmlsgQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV----QRLQECIAELSQQLGT 864
Cdd:COG1196 259 EAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 865 SEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSEtckgseqvhklEEEL 944
Cdd:COG1196 335 LEEELEELEEELEEA--------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 945 EAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREK 1024
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907081936 1025 EEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQ 1068
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
643-924 |
1.06e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 643 SERLSTHELtSLLEKELEQSQKEASDLLEQNRLLQDQLRvALGREQSAREGYVLQTEVATSPsgawqrLHRVNQDLQSEL 722
Cdd:TIGR02168 219 KAELRELEL-ALLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSE------LEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 723 EAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEqgkvREQLEEWQHS 802
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 803 KAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDR----QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKR 878
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907081936 879 NYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQK 924
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
707-1072 |
6.38e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 707 AWQRLHRVNQDLQSELEaqcRRQELITQQiqtlkhsyGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELK 786
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIE---RLEKFIKRT--------ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 787 mEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-----------------QALQRDRQKEVQ 849
Cdd:PRK03918 232 -ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 850 RLQECIAELSQQL-GTSEQAQRLMEKKLKrnytllLESCEQEKQALLQNLKEVEDKASAYED------QLQGHVQQVEAL 922
Cdd:PRK03918 311 EIEKRLSRLEEEInGIEERIKELEEKEER------LEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 923 QKEKLSETCKGSEQVHKLEEELEAREAS-IRQLAQHVQSLHDE---------------RDLIKHQFQELMER----VATS 982
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITArIGELKKEIKELKKAieelkkakgkcpvcgRELTEEHRKELLEEytaeLKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 983 DGDVAELQEKLRGKEVDYQNLEHSHHRVS--VQLQSVRTLLREKEEELKHI------------KETHERV--LEKKDQDL 1046
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYnleelekkaeeyEKLKEKLikLKGEIKSL 544
|
410 420
....*....|....*....|....*.
gi 1907081936 1047 NEALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEE 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-1104 |
7.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNQDLQ------SELEAQCRRqeLITQQIQTLKhsYGEAKDAIRHHEAEIQTLQtrlgnaaaelaiKEQALAKLK 782
Cdd:TIGR02168 179 RKLERTRENLDrledilNELERQLKS--LERQAEKAER--YKELKAELRELELALLVLR------------LEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 783 gELKMEQGKVREQLEEwqhskamLSGQLRASEQKLRSTEARLLEKTQELRDLetqqalqrdrQKEVQRLQECIAELSQQL 862
Cdd:TIGR02168 243 -ELQEELKEAEEELEE-------LTAELQELEEKLEELRLEVSELEEEIEEL----------QKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 863 GTSEQAQRLMEKKLKRnYTLLLESCEQEKQALLQNLKEVEDKasayEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEE 942
Cdd:TIGR02168 305 QILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 943 EleareasIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEklrgkevdyQNLEHSHHRVSVQLQSVRTLLR 1022
Cdd:TIGR02168 380 Q-------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ---------EIEELLKKLEEAELKELQAELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1023 EKEEELKHIKETHERV---LEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLRRFvSDSPKDAKEPLsttEPTEEGS 1099
Cdd:TIGR02168 444 ELEEELEELQEELERLeeaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENL-EGFSEGVKALL---KNQSGLS 519
|
....*
gi 1907081936 1100 GILPL 1104
Cdd:TIGR02168 520 GILGV 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-866 |
1.52e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 657 KELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPsgAWQRLHRVN------QDLQSELEAQCRRQE 730
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLElleaelEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 731 LITQQIQTLKHSYGEAKDAIRHH--------EAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHS 802
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081936 803 KAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV-QRLQECIAELSQQLGTSE 866
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAEALGLDE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
754-1062 |
2.45e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 754 EAEIQTLQTRLGNAAAELAIKEQALAKLKGE---LKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQE 830
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 831 LRDLETQ-QALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYE 909
Cdd:TIGR02168 756 LTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 910 DQLQGHVQQVEALQKEKLSEtckgSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAEL 989
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 990 QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEEL----KHIKETHERVLEKKDQDLNEALVKMIALGSSLEE 1062
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
774-1072 |
2.59e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 774 KEQALAKLKGELKMEQGKVREQLEEwqhsKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQqaLQRDRQkEVQRLQE 853
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKD--LARLEA-EVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 854 CIAELSQQLgtSEQAQRLMEKKLKrnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEkLSETckg 933
Cdd:TIGR02168 748 RIAQLSKEL--TELEAEIEELEER------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLL--- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 934 SEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQ 1013
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081936 1014 LQSVRTLLREKE----------EELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:TIGR02168 896 LEELSEELRELEskrselrrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
48-145 |
2.92e-09 |
|
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 56.01 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 48 GWLLLAPDGTdfdnpvhrSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEaRTGQKFSLCILTPDKE 127
Cdd:cd00821 3 GYLLKRGGGG--------LKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIPLSGILEVEEVS-PKERPHCFELVTPDGR 73
|
90
....*....|....*....
gi 1907081936 128 HF-IRAETKEIISGWLEML 145
Cdd:cd00821 74 TYyLQADSEEERQEWLKAL 92
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
791-1075 |
3.67e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 791 KVREQLEEWQHSKAMLsgQLRASEQKLRSTEARLLEKTQELRDLETQQALqrdRQKEVQRLQECIAELSQQLGTSEQAQR 870
Cdd:COG1196 217 ELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 871 LMEKKLKRnytlllesCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETckgsEQVHKLEEELEAREAS 950
Cdd:COG1196 292 ELLAELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 951 IRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKH 1030
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907081936 1031 IKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLR 1075
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1912-2177 |
4.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1912 AAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQH- 1990
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRREl 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1991 QRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2070
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2071 YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLtgdgggestglpltqgKDAYELEVLL 2150
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA----------------EEEAELEEEE 458
|
250 260
....*....|....*....|....*..
gi 1907081936 2151 RVKESEIQYLKQEISSLKDELQTALRD 2177
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-1070 |
1.23e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKme 788
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 789 qgKVREQLEEWQHSKAMLSGQLRASEQKLRstEARLLEKTQELRDLEtqqalqrdrqKEVQRLQECIAELSQQLGTSEQA 868
Cdd:TIGR02169 762 --ELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE----------EEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 869 QRLMEKKLkrnytlllesceQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEARE 948
Cdd:TIGR02169 828 KEYLEKEI------------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 949 ASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELqEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEE-E 1027
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvN 974
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907081936 1028 LKHIKEtHERVLEKKDqDLNEALVKMIALGSSLEETEIKLQEK 1070
Cdd:TIGR02169 975 MLAIQE-YEEVLKRLD-ELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
793-1097 |
1.60e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 793 REQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQalqRDRQKEVQRLQEciaelsqqlgtSEQAQRLM 872
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI---GEIEKEIEQLEQ-----------EEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 873 EKKLKRNytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEAL-QKEKLSETCKGSEQVHKLEEELEAREASI 951
Cdd:TIGR02169 739 LEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 952 RQLAQHVQSLHDERDLIKHQFQELMERVatsdgDVAELQEKLRGKEVDyqNLEHSHHRVSVQLQSVRTLLREKEEELKHI 1031
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQR-----IDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081936 1032 K------ETHERVLEKKDQDLNEALVKmiaLGSSLEETEIKLQEKEECLRRFvsDSPKDAKEPLSTTEPTEE 1097
Cdd:TIGR02169 888 KkerdelEAQLRELERKIEELEAQIEK---KRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLE 954
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
44-145 |
1.75e-08 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 54.09 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCT-DVVDGEARTGQKFSLCI 121
Cdd:smart00233 1 VIKEGWLYKKSGG--------GKKSWKKRYFVLFNSTLLYYKSKKDKKSYkPKGSIDLSGCTvREAPDPDSSKKPHCFEI 72
|
90 100
....*....|....*....|....*
gi 1907081936 122 LTPDKE-HFIRAETKEIISGWLEML 145
Cdd:smart00233 73 KTSDRKtLLLQAESEEEREKWVEAL 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
709-925 |
2.24e-08 |
|
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: 58.62 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNQDL---QSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGEl 785
Cdd:COG4942 27 AELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 786 kmeqgkvreqleewqhskamLSGQLRASEQKLRSTEARLL----EKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQ 861
Cdd:COG4942 106 --------------------LAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 862 LGTSEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKE 925
Cdd:COG4942 166 RAELEAERAELEALLAEL--------EEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
755-926 |
5.77e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 755 AEIQTLQTRLGNAAAELAIKEQALAKLKgELKMEQGKVREQLEEWQHSKAMLSGQLRASE--QKLRSTEARLLEKTQELR 832
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 833 DLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQL 912
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....
gi 1907081936 913 QGHVQQVEALQKEK 926
Cdd:COG4717 230 EQLENELEAAALEE 243
|
|
| PH2_MyoX |
cd13296 |
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular ... |
48-145 |
6.94e-08 |
|
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270108 Cd Length: 103 Bit Score: 52.47 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 48 GWLLLAPDGTdfdNPVHRsRKWQRRFFILYEHGLLRYALDEmPTTLPQGTINMNQCTDVVDgeaRTGQKFSLCILTPDKE 127
Cdd:cd13296 3 GWLTKKGGGS---STLSR-RNWKSRWFVLRDTVLKYYENDQ-EGEKLLGTIDIRSAKEIVD---NDPKENRLSITTEERT 74
|
90
....*....|....*...
gi 1907081936 128 HFIRAETKEIISGWLEML 145
Cdd:cd13296 75 YHLVAESPEDASQWVNVL 92
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
811-1072 |
7.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 811 RASEQKLRSTEARLL-------EKTQELRDLETQ-------QALQ---RDRQKEVQRLQecIAELSQQLGTSEQAQRLME 873
Cdd:COG1196 175 EEAERKLEATEENLErledilgELERQLEPLERQaekaeryRELKeelKELEAELLLLK--LRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 874 KKLKRnYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETckgsEQVHKLEEELEAREASIRQ 953
Cdd:COG1196 253 AELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 954 LAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEvdyQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKE 1033
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907081936 1034 ThERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:COG1196 405 L-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1923-2115 |
1.04e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1923 LRERIQELEAQMGVMREELGH-----KELEGDVAALQEKyqrdFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKL 1997
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEElesklDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1998 REEKDRLLAEETAATIsaieamkNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLE 2077
Cdd:TIGR02168 383 TLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081936 2078 NAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAA 2115
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
734-924 |
1.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 734 QQIQTLKHSYGEAKDAIRHHEA--EIQTLQTRLGNAAAELAIKEQALAKLK--------GELKMEQGKVREQLEEWQHSK 803
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 804 AMLSGQLRASEQKLRSTEARLLE-KTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTL 882
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907081936 883 LLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQK 924
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
649-1098 |
1.70e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.72 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 649 HELTSLLEKELEQSQKEASDLLEQNRLLQDqLRVALGREQSAREGyvLQTEVATSPS----------------GAWQRLH 712
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQD-LEEQLDEEEAARQK--LQLEKVTTEAkikkleedillledqnSKLSKER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 713 RVNQDLQSELEAQCRRQELITQQIQTLKHSygeakdairhHEAEIQTLQTRLGNAAAelaiKEQALAKLKGELKMEQGKV 792
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNK----------HEAMISDLEERLKKEEK----GRQELEKAKRKLEGESTDL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 793 REQLEEWQHSKAMLSGQLRASEQKLRSTEARLlektqelrdlETQQALQRDRQKEVQRLQECIAELSQQLgTSEQAQRLM 872
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARL----------EEETAQKNNALKKIRELEAQISELQEDL-ESERAARNK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 873 EKKLKRNYTLLLESCEQEKQALL------QNLK-----EVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLE 941
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLdttaaqQELRskreqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 942 EELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLL 1021
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1022 REKEEelKHIKETHE-RVLEKKDQD----LNEALVKMIALGSSLEETEI-------KLQEKEECLRRF----------VS 1079
Cdd:pfam01576 450 NEAEG--KNIKLSKDvSSLESQLQDtqelLQEETRQKLNLSTRLRQLEDernslqeQLEEEEEAKRNVerqlstlqaqLS 527
|
490
....*....|....*....
gi 1907081936 1080 DSPKDAKEPLSTTEPTEEG 1098
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEG 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1911-2177 |
1.73e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1911 PAAKDEAESMSGLRERIQELEAQMGVMREELGHkeLEgDVAALQEKYQRDFESLKA--TCERGFAAmeETHQKKIEDLQR 1988
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIEL--LE-PIRELAERYAAARERLAEleYLRAALRL--WFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1989 qhqrELEKLREEKDRLLAEETAATISAIEAmkNAHREEMERELEKSQRSQISSINSDIEALRRqyleELQSVQRELEVLS 2068
Cdd:COG4913 296 ----ELEELRAELARLEAELERLEARLDAL--REELDELEAQIRGNGGDRLEQLEREIERLER----ELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2069 EQysqkcLENAHLAQALEAE--RQALRQCQRENQELNAHNQELNNRLAAEITRLRtlltgdgggestglpltqgkdayEL 2146
Cdd:COG4913 366 AL-----LAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALR-----------------------DL 417
|
250 260 270
....*....|....*....|....*....|.
gi 1907081936 2147 EVLLRVKESEIQYLKQEISSLKDELQTALRD 2177
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1929-2223 |
2.59e-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: 56.23 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1929 ELEAQMGVMREELGhkELEGDVAALQEKyqrdFESLKATCERGFAAMEETHqKKIEDLQRQHQRELEKLREEKDRLlaEE 2008
Cdd:TIGR02169 671 SEPAELQRLRERLE--GLKRELSSLQSE----LRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERL--EE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2009 TAATISAIEAMKNAHREEMErELEK---SQRSQISSINSDIEALRRQYLEE-LQSVQRELEVLSEQYSQKCLENAHLAQA 2084
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELK-ELEArieELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2085 LEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEStglpltqgkDAYELEVLLRVKESEIQYLKQEI 2164
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE---------ELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081936 2165 SSLKDELQTALRDKKYASDKYKDIYTELSIAKAKAdcdiSRLKEQLKAATEALGEKSPE 2223
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKL----EALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1738-2099 |
2.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1738 QAVGALKEEYEELLhkqksEYQKVITliEKENTELKAKVSQMDHQQRCLQEAENKHSESmfalqgryEEEIRCMVEQLSH 1817
Cdd:TIGR02169 198 QQLERLRREREKAE-----RYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASL--------EEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1818 TENTLqAERSRVLSQLDASVKDRQAMEQHHVQ--------QMKMLEDRFQLKVRELQ------AVHQEELRALQEHyIWS 1883
Cdd:TIGR02169 263 LEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKekigeleaEIASLERSIAEKERELEdaeerlAKLEAEIDKLLAE-IEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1884 LRGALSLYQpshpdsslapgpSEPRAVPAA-KDEAESMSGLRERIQELEAQMGVMREELghkelegdvaalqEKYQRDFE 1962
Cdd:TIGR02169 341 LEREIEEER------------KRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDEL-------------KDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1963 SLKatcergfaameethqKKIEDLQRQHQRELEKLREEKDRLlaEETAATISAIEAMKNAHREEME--RELEKSQRSQIS 2040
Cdd:TIGR02169 396 KLK---------------REINELKRELDRLQEELQRLSEEL--ADLNAAIAGIEAKINELEEEKEdkALEIKKQEWKLE 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081936 2041 SINSDIEALRRQYL---EELQSVQRELEVLSEQYSQkclenahlaqaLEAERQALRQCQREN 2099
Cdd:TIGR02169 459 QLAADLSKYEQELYdlkEEYDRVEKELSKLQRELAE-----------AEAQARASEERVRGG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
610-855 |
3.75e-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: 55.84 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 610 VEIEQRWHQVET--TPLREEKQVPIAPLHLSLEdrSERLSTHELTSLLEKELEQSQKE-ASDLLEQNRLLQD--QLRVAL 684
Cdd:TIGR02169 268 EEIEQLLEELNKkiKDLGEEEQLRVKEKIGELE--AEIASLERSIAEKERELEDAEERlAKLEAEIDKLLAEieELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 685 GREQSAREGyvLQTEVATSPsgawQRLHRVNQDLQS-ELEAQCRRQEL--ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQ 761
Cdd:TIGR02169 346 EEERKRRDK--LTEEYAELK----EELEDLRAELEEvDKEFAETRDELkdYREKLEKLKREINELKRELDRLQEELQRLS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 762 TRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSG---QLRASEQKLRSTEARLLEKTQELRDLETQQ 838
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKyeqELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
250
....*....|....*..
gi 1907081936 839 ALQRDRQKEVQRLQECI 855
Cdd:TIGR02169 500 RASEERVRGGRAVEEVL 516
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
44-145 |
4.34e-07 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 50.25 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCTDV-VDGEARTGQKFSLCI 121
Cdd:pfam00169 1 VVKEGWLLKKGGG--------KKKSWKKRYFVLFDGSLLYYKDDKSGKSKePKGSISLSGCEVVeVVASDSPKRKFCFEL 72
|
90 100
....*....|....*....|....*...
gi 1907081936 122 LTPD----KEHFIRAETKEIISGWLEML 145
Cdd:pfam00169 73 RTGErtgkRTYLLQAESEEERKDWIKAI 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1805-2102 |
5.22e-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: 55.46 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1805 EEEIRCMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLE--DRFQLKVRELQAVHQEELRALQehyiw 1882
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqlEQEEEKLKERLEELEEDLSSLE----- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1883 slrgalslyqpshpdsslapgpsepRAVPAAKDEaesMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKyQRDFE 1962
Cdd:TIGR02169 751 -------------------------QEIENVKSE---LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI-QAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1963 SLKATCERGFAAMEETHQKkiedLQRQHQRE--LEKLREEK--DRLLAEETAATISAIEAMKNAHREEMERELEKSQRS- 2037
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQK----LNRLTLEKeyLEKEIQELqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAl 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 2038 -QISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQEL 2102
Cdd:TIGR02169 878 rDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
627-1032 |
5.30e-07 |
|
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: 55.12 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 627 EKQVPIAPLHLSlEDRSER----LSTHELTSLLEK---ELEQSQKEASDLLEQNRLLQDQ-LRVALGREQSAREGYVLQT 698
Cdd:pfam15921 348 EKQLVLANSELT-EARTERdqfsQESGNLDDQLQKllaDLHKREKELSLEKEQNKRLWDRdTGNSITIDHLRRELDDRNM 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 699 EVatspsgawQRLHRVNQDLQSELEAQCRRQ--------------ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRL 764
Cdd:pfam15921 427 EV--------QRLEALLKAMKSECQGQMERQmaaiqgkneslekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 765 GNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHskamlsgqLRASEQKLRSTEArllektqELRDLETQQAlQRDR 844
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQT-------ECEALKLQMA-EKDK 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 845 QKEVQRLQ-ECIAELSQQLGTSEQAQRLMEKKLKRNYtlllesceQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEaLQ 923
Cdd:pfam15921 563 VIEILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEI--------NDRRLELQEFKILKDKKDAKIRELEARVSDLE-LE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 924 KEKLSETckGSEQVhkleeeleareasirqlaQHVQSLHDERDlikhqfqELMERVATSDGDVAELQEKLRGKEVDYQN- 1002
Cdd:pfam15921 634 KVKLVNA--GSERL------------------RAVKDIKQERD-------QLLNEVKTSRNELNSLSEDYEVLKRNFRNk 686
|
410 420 430
....*....|....*....|....*....|...
gi 1907081936 1003 ---LEHSHHRVSVQLQSVRTLLREKEEELKHIK 1032
Cdd:pfam15921 687 seeMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1921-2219 |
5.75e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1921 SGLRERIQELEAQMGVMREELG-----HKELEGDVAALQE---------KYQRDFESLKAtcergfaameETHQKKIEDL 1986
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLErlediLGELERQLEPLERqaekaeryrELKEELKELEA----------ELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1987 QRQHQRELEKLREEKDRL--LAEETAATISAIEAMKNAHREEMERELEKSQR-----SQISSINSDIEAL---RRQYLEE 2056
Cdd:COG1196 238 EAELEELEAELEELEAELeeLEAELAELEAELEELRLELEELELELEEAQAEeyellAELARLEQDIARLeerRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2057 LQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDgggestglp 2136
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2137 LTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEA 2216
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
...
gi 1907081936 2217 LGE 2219
Cdd:COG1196 469 LEE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
755-1095 |
7.01e-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: 55.07 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 755 AEIQTLQTRLGNAAAELAIKEQALAKLKGElkmeqgkvREQLEEWQHskamLSGQLRASEQKLRSTEARLLEKTQE--LR 832
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE--------REKAERYQA----LLKEKREYEGYELLKEKEALERQKEaiER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 833 DLETQQALQRDRQKEVQRLQECIAELSQQLgtSEQAQRLMEKKLKRNYTLllesceQEKQALLQ-NLKEVEDKASAYEDQ 911
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLL--EELNKKIKDLGEEEQLRV------KEKIGELEaEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 912 LQghvqQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQE 991
Cdd:TIGR02169 317 LE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 992 KLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETH---ERVLEKKDQDLNEALVKMIALGSSLEETEIKLQ 1068
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340
....*....|....*....|....*..
gi 1907081936 1069 EKEECLRRfVSDSPKDAKEPLSTTEPT 1095
Cdd:TIGR02169 473 DLKEEYDR-VEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1846-2172 |
1.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1846 HHVQQMKMLEDRFQLKVRELQAVhQEELRALQEhyiwSLRGALSLYQPSHPDSSLAPGPSEpRAVPAAKDEAESMSGLRE 1925
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAEL-RKELEELEE----ELEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1926 RIQELEAQMGVMREELGH-----KELEGDVAALQEKYQRDFESLKATCERgfaameethqkkIEDLQRQHQRELEKLREE 2000
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEaeeelAEAEAEIEELEAQIEQLKEELKALREA------------LDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2001 KDRLLAEETAAtisaieAMKNAHREEMERELEKsQRSQISSINSDIEALRRQyLEELQSvqrELEVLSEQYSQKCLENAH 2080
Cdd:TIGR02168 823 RERLESLERRI------AATERRLEDLEEQIEE-LSEDIESLAAEIEELEEL-IEELES---ELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2081 LAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLltgdgggESTGLPLTQ-----GKDAYE-LEVLLRVKE 2154
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQErlseeYSLTLEeAEALENKIE 964
|
330
....*....|....*...
gi 1907081936 2155 SEIQYLKQEISSLKDELQ 2172
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1766-2151 |
1.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1766 EKENTELKAKVSQMDHQQRCLQEAENKHSESmfalqgryEEEIRCMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQ 1845
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLE-LEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1846 HHVQQMKMLEDRFQLKVRELQAVHQEELRALQEhyiwslrgalslyqpshpdsslapgpsepravpaakdEAEsmsgLRE 1925
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEE-------------------------------------LAE----LEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1926 RIQELEAQMGVMREELghKELEGDVAALQEKYQRdfeslkatcergfaamEETHQKKIEDLQRQHQRELEKLREEKDRLL 2005
Cdd:COG1196 331 ELEELEEELEELEEEL--EEAEEELEEAEAELAE----------------AEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2006 AEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQAL 2085
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081936 2086 EAERQALRQCQRENQELNA-----HNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLR 2151
Cdd:COG1196 473 ALLEAALAELLEELAEAAArllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
655-865 |
1.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRL--LQDQLRVALGREQSAREGYV-LQTEVAtspsGAWQRLHRVNQDLQSELEAQcrRQEL 731
Cdd:COG3206 187 LRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAeARAELA----EAEARLAALRAQLGSGPDAL--PELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 732 ITQQIQTLKHSYGEAkdairhhEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLE-EWQHSKAMLSgQL 810
Cdd:COG3206 261 QSPVIQQLRAQLAEL-------EAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREA-SL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 811 RASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKE-VQRLQEciAELSQQLGTS 865
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEE--ARLAEALTVG 386
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-1027 |
2.30e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSARegyvLQTEVATSPSG---------AWQRLHRVNQDLQSEL-EA 724
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEA----LEAELAELPERleeleerleELRELEEELEELEAELaEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 725 QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLkgELKMEQGKVREQLEEWQHSKA 804
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 805 MLSGQL------------------------------RASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQEC 854
Cdd:COG4717 254 IAAALLallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 855 I--AELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQ-----NLKEVEDKASAYED--QLQGHVQQVEALQKE 925
Cdd:COG4717 334 LspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagveDEEELRAALEQAEEyqELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 926 KLSETCKGSEQVHKLE--EELEAREASIRQLAQHVQSLHDERDLIKHQFQELMErvatsDGDVAELQEKLRGKEVDYQNL 1003
Cdd:COG4717 414 LLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELREL 488
|
410 420
....*....|....*....|....
gi 1907081936 1004 EHSHHRVSVQLQSVRTLLREKEEE 1027
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-1076 |
2.52e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 611 EIEQRWHQVETTPLREEKQvpIAPLHLSLEDRSERL-STHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQS 689
Cdd:COG1196 285 EAQAEEYELLAELARLEQD--IARLEERRRELEERLeELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 690 AREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAA 769
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 770 ELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSgQLRASEQKLRSTEARLLE--KTQELRDLETQQALQRDRQKE 847
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEaeADYEGFLEGVKAALLLAGLRG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 848 VQR---------------LQECIAELSQQLGT------SEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKAS 906
Cdd:COG1196 522 LAGavavligveaayeaaLEAALAAALQNIVVeddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 907 AYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELME---RVATSD 983
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAallEAEAEL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 984 GDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEET 1063
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
490
....*....|...
gi 1907081936 1064 EIKLQEKEECLRR 1076
Cdd:COG1196 762 LEELERELERLER 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-997 |
2.93e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 767 AAAELAIKEQALAKLKGELKmeqgKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQ 845
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 846 KEVQRLQECIAELSQQLgtseqaqRLMEKKLKRNYTLLLESCEQEKQAL--LQNLKEVEDKASAYEDQLQGHVQQVEALQ 923
Cdd:COG4942 94 ELRAELEAQKEELAELL-------RALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 924 KEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKE 997
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PH_Gab-like |
cd13324 |
Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are ... |
45-141 |
3.07e-06 |
|
Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. There are 3 families: Gab1, Gab2, and Gab3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270133 Cd Length: 112 Bit Score: 48.18 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 45 IYGGWLLLAPdgtdfdnPVHR--SRKWQRRFFILYEHGL------LRYALDEMPTTlPQGTINMNQCTDVVDGEARTGQK 116
Cdd:cd13324 2 VYEGWLTKSP-------PEKKiwRAAWRRRWFVLRSGRLsggqdvLEYYTDDHCKK-LKGIIDLDQCEQVDAGLTFEKKK 73
|
90 100
....*....|....*....|....*....
gi 1907081936 117 FS----LCILTPDKEHFIRAETKEIISGW 141
Cdd:cd13324 74 FKnqfiFDIRTPKRTYYLVAETEEEMNKW 102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
770-1071 |
3.31e-06 |
|
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 coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 770 ELAIKEQALAKL------KGELKMEQGKVREQL--EEWQHSKAMLSGQLRASEQKLRSTEARLLEKT---QELRDLETQQ 838
Cdd:pfam02463 167 LKRKKKEALKKLieetenLAELIIDLEELKLQElkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKlneERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 839 ALQRDRQKEVQRLQECIAELSQQ----LGTSEQAQRLMEKKLKRNYTLL------LESCEQEKQALLQNLKEVEDKASAY 908
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQvlkeNKEEEKEKKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 909 EDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQ---FQELMERVATSDGD 985
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAaklKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 986 VAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEI 1065
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
....*.
gi 1907081936 1066 KLQEKE 1071
Cdd:pfam02463 487 ELLLSR 492
|
|
| PH_PLEKHD1 |
cd13281 |
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ... |
64-145 |
3.84e-06 |
|
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270099 Cd Length: 139 Bit Score: 48.47 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 64 HRSRKWQRRFFILYEHGLLRYALDEMPT--------TLPQGTINMNQCTDVVDGEarTGQKFSLCILTPD--KEHFIRAE 133
Cdd:cd13281 25 HQSAKWSKRFFIIKEGFLLYYSESEKKDfektrhfnIHPKGVIPLGGCSIEAVED--PGKPYAISISHSDfkGNIILAAD 102
|
90
....*....|..
gi 1907081936 134 TKEIISGWLEML 145
Cdd:cd13281 103 SEFEQEKWLDML 114
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1991-2219 |
5.10e-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: 51.98 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1991 QRELEKLREEKDRLLAEETAATISAIEAMKNahREEMERELEKSQRsQISSINSDIEALRRQYLEELQSVQR---ELEVL 2067
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK-ELEELSRQISALRKDLARLEAEVEQleeRIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2068 SEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTL-----LTGDGGGESTGLPLTQGKD 2142
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 2143 AYELEVLLRVKESEIQYLKQEISSLKDElqtaLRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGE 2219
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
640-969 |
6.72e-06 |
|
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: 51.61 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 640 EDRSERLSTheLTSLLEKELEQSQKEASDLLEQNrllqdqlrvALGREQSAREGYVLqtevatspSGAWQRLHRVNQDLQ 719
Cdd:TIGR02169 183 EENIERLDL--IIDEKRQQLERLRREREKAERYQ---------ALLKEKREYEGYEL--------LKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 720 SELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQ--------TLQTRLGNAAAELAIKEQALAKLKGELKMEQGK 791
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 792 VR---EQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-----QALQRDRQKEVQRlQECIAELSQQLG 863
Cdd:TIGR02169 324 LAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdKEFAETRDELKDY-REKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 864 TSEQAQ-RLMEKKLKRNYTLL-----LESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKL---SETCKGS 934
Cdd:TIGR02169 403 ELKRELdRLQEELQRLSEELAdlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYdlkEEYDRVE 482
|
330 340 350
....*....|....*....|....*....|....*
gi 1907081936 935 EQVHKLEEELEAREASIRQLAQHVQSLHDERDLIK 969
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| PH_Gab2_2 |
cd13384 |
Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily ... |
45-141 |
6.82e-06 |
|
Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. Members here include insect, nematodes, and crustacean Gab2s. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 241535 Cd Length: 115 Bit Score: 47.05 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 45 IYGGWLLLAPdgtdfdnPVHR--SRKWQRRFFILY-----EHGLLRYALDEMPTTLpQGTINMNQCTDV-----VDGEAR 112
Cdd:cd13384 4 VYEGWLTKSP-------PEKRiwRAKWRRRYFVLRqseipGQYFLEYYTDRTCRKL-KGSIDLDQCEQVdagltFETKNK 75
|
90 100
....*....|....*....|....*....
gi 1907081936 113 TGQKFSLCILTPDKEHFIRAETKEIISGW 141
Cdd:cd13384 76 LKDQHIFDIRTPKRTYYLVADTEDEMNKW 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
793-1029 |
7.67e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 793 REQLEEWQHSKAMLSgQLRASEQKLRSTEARLlEKTQELRD----------LETQQALQRDRQKEVQRLQECIAELSQQL 862
Cdd:COG4913 241 HEALEDAREQIELLE-PIRELAERYAAARERL-AELEYLRAalrlwfaqrrLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 863 GTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQghvqqvealqkeKLSETCKGSEQVHKLEE 942
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA------------ALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 943 eleareasiRQLAQHVQSLHDERDlikhqfqELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLR 1022
Cdd:COG4913 387 ---------AEAAALLEALEEELE-------ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
250
....*....|.
gi 1907081936 1023 E----KEEELK 1029
Cdd:COG4913 451 EalglDEAELP 461
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
734-1064 |
8.49e-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: 51.17 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 734 QQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAI---KEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQL 810
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 811 RASEQKLRSTEA-----RLLEKtqELRDLETQQA-LQRDRQKEVQRLQECIAELSQqlgTSEQAQRLMEKKLKRNYTLll 884
Cdd:TIGR04523 197 LKLELLLSNLKKkiqknKSLES--QISELKKQNNqLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDEQNKIKKQL-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 885 esceQEKQallQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKG--------SEQVHKLEEELEAREASIRQLAQ 956
Cdd:TIGR04523 270 ----SEKQ---KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLNE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 957 HVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKhIKETHE 1036
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-KLQQEK 421
|
330 340
....*....|....*....|....*...
gi 1907081936 1037 RVLEKKDQDLNEALVKMIALGSSLEETE 1064
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
654-901 |
8.49e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 654 LLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQ----CRRQ 729
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 730 ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAikeqalaklkgELKMEQGKVREQLEEWQHSKAMLSGQ 809
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-----------RMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 810 LRASEQKLRSTEARLlektQELRDLETQQALQrdrqkeVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTL--LLESC 887
Cdd:pfam07888 180 LQQTEEELRSLSKEF----QELRNSLAQRDTQ------VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLqeRLNAS 249
|
250
....*....|....
gi 1907081936 888 EQEKQALLQNLKEV 901
Cdd:pfam07888 250 ERKVEGLGEELSSM 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1950-2259 |
1.07e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1950 VAALQEKYQRDFESLKATCERgfaamEETHQKKIEDLQRQhqreLEKLREEKDRLL--------AEETAATI--SAIEAM 2019
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEEN-----IERLDLIIDEKRQQ----LERLRREREKAEryqallkeKREYEGYEllKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2020 K------NAHREEMERELEKSQRsQISSINSDIEALRRqyleELQSVQRELEVLSEQYSQKCLENAHLAQA-LEAERQAL 2092
Cdd:TIGR02169 236 ErqkeaiERQLASLEEELEKLTE-EISELEKRLEEIEQ----LLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2093 RQCQRENQELNAHNQELN---NRLAAEITRLRTLLtgdgggESTGLPLTQGKDAY-ELEVLLRVKESEIQYLKQEISSLK 2168
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEaeiDKLLAEIEELEREI------EEERKRRDKLTEEYaELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2169 DELQTALRDKKYASDKYKDIYTELSI---AKAKADCDISRLKEQLKAATEALGEkSPEGTTVSGYDIMKSKSNPDFLKKD 2245
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAAD 463
|
330
....*....|....
gi 1907081936 2246 RSCVTRQLRNIRSK 2259
Cdd:TIGR02169 464 LSKYEQELYDLKEE 477
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
655-1072 |
1.46e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRVaLGREQSAREGYVLQTEvatspsgaWQRLhRVNQDLqSELEAQCRRQELITQ 734
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNL-LEKEKLNIQKNIDKIK--------NKLL-KLELLL-SNLKKKIQKNKSLES 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 735 QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAikeqalaklkgELKMEQGKVREQLEEWQHskamlsgQLRASE 814
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-----------QLKDEQNKIKKQLSEKQK-------ELEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 815 QKLRSTEARLLEKTQELRDL--ETQQALQRDRQKEVQRLQECIAELSQQLGTSEQA-QRLMEK--KLKRNytllLESCEQ 889
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQisQLKKE----LTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 890 EKQALLQNLKEVEDKASAYEDQLQGHVQQVEAL--QKEKLSETCKGSEQVHKleeeleareasirQLAQHVQSLHDERDL 967
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQ-------------QKDEQIKKLQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 968 IKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNL--------------EHSHHRVSVQLQSVRTLLREKEEELKHIKE 1033
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907081936 1034 tHERVLEKKDQDLN----EALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:TIGR04523 504 -EKKELEEKVKDLTkkisSLKEKIEKLESEKKEKESKISDLED 545
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1734-2167 |
1.84e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1734 QKRAQAVGALKEEYEELLHKQKSEYQKVITLIEKENTELKAKVSQMDHQQRCLQEAEN--KHSESMFALQGRYEEEIRCM 1811
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEEL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1812 VEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKmLEDRFQLKVRELQAVHQEELRALQEHyiWSLRGALSLY 1891
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAARL--LLLLEAEADY 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1892 QPSHPDSSLAPGPSEPRAVPAAKDEAesMSGLRERIQELEAQMGVMREELGHKELEgdVAALQEKYQRDFESLKAT---- 1967
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVL--IGVEAAYEAALEAALAAALQNIVVEDDE--VAAAAIEYLKAAKAGRATflpl 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1968 --CERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRL---LAEETAATISAIEAMKNAHREEMERELEKSQRSQISSI 2042
Cdd:COG1196 580 dkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2043 NSDIEALRRQYLEELQSVQRELEVLSEQ--YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRL 2120
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERlaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907081936 2121 RTLltgdgggESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSL 2167
Cdd:COG1196 740 ELL-------EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
639-979 |
2.43e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 639 LEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQtevatspsgawQRLHRVNQDL 718
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ-----------EKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 719 QsELEAQCRRQELITQQIQTLKHSYGEAKDAIrhhEAEIQTLQTRLGNAAAELAIKE----------QALAKLK---GEL 785
Cdd:PRK04863 358 E-ELEERLEEQNEVVEEADEQQEENEARAEAA---EEEVDELKSQLADYQQALDVQQtraiqyqqavQALERAKqlcGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 786 KMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEA--RLLEKTQEL-----------------RDLETQQALQRDRQK 846
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahSQFEQAYQLvrkiagevsrseawdvaRELLRRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 847 EVQRLQECIAELSQQLGTSEQAQRLM---EKKLKRNYTL--LLESCEQEKQALLQNLKE----VEDKASAYEDQLQGHVQ 917
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLaefCKRLGKNLDDedELEQLQEELEARLESLSEsvseARERRMALRQQLEQLQA 593
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081936 918 QVEALQK---------EKLSETCkgsEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERV 979
Cdd:PRK04863 594 RIQRLAArapawlaaqDALARLR---EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
822-1072 |
2.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 822 ARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKklkrnytlllescEQEKQALLQNLKEV 901
Cdd:COG4913 194 LRLLHKTQSFKPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALED-------------AREQIELLEPIREL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 902 EDKASAYEDQLQGHVQQVEALQKEKlsetckGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVAT 981
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWF------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 982 SDGD-VAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSL 1060
Cdd:COG4913 335 NGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250
....*....|..
gi 1907081936 1061 EETEIKLQEKEE 1072
Cdd:COG4913 415 RDLRRELRELEA 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1756-2225 |
3.45e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1756 SEYQKVITLIEKENTELKAKVSQMDHQQRCLQ-EAENK-------HSESMFALQGRYEEEIRCMVEQLSHTENTLQAERS 1827
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALKsESQNKielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1828 RvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEHYIWSlrgalslyqpshpDSSLAPGPSEp 1907
Cdd:pfam15921 300 Q-LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLA-------------NSELTEARTE- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1908 ravpaaKDEAESMSG-LRERIQELEAQMGVMREELG---------------------HKELEGDVAALQ-EKYQRDFESL 1964
Cdd:pfam15921 365 ------RDQFSQESGnLDDQLQKLLADLHKREKELSlekeqnkrlwdrdtgnsitidHLRRELDDRNMEvQRLEALLKAM 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1965 KATC----ERGFAAMEETHQ--KKIEDLQRQHQRELEKLREEKDRLLA-----EETAATISAIeamkNAHREEMERELEK 2033
Cdd:pfam15921 439 KSECqgqmERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERTVSDL----TASLQEKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2034 SQrSQISSINS--DIEALRRQYL----EELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQ 2107
Cdd:pfam15921 515 TN-AEITKLRSrvDLKLQELQHLknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2108 ELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLRVKESE-----IQYLKQEISSLKDELQTALRDKKYAS 2182
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSerlraVKDIKQERDQLLNEVKTSRNELNSLS 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907081936 2183 DKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGE-----KSPEGT 2225
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlKSMEGS 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
655-868 |
4.19e-05 |
|
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: 48.22 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLrvalgrEQSAREGYVLQTEVATspsgAWQRLHRVNQDLQSELEAQCRRQELITQ 734
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRI------AALARRIRALEQELAA----LEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 735 QIQTL----KHSY-------GEAKDAIRHHEAeIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSK 803
Cdd:COG4942 109 LLRALyrlgRQPPlalllspEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081936 804 AMLSGQLRASEQKLRSTEARLLEKTQELRDLetqqalqrdrQKEVQRLQECIAELSQQLGTSEQA 868
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAEL----------QQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
640-1072 |
4.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 640 EDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYvlqTEVATSPSGAWQRLHRVNQDLQ 719
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---REDADDLEERAEELREEAAELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 720 SELEAqCRRQelitqqiqtlkhsYGEAKDAIRHHEAEIQTLQTRLGNAAAELaikeQALAKLKGELKMEQGKVREQLEEw 799
Cdd:PRK02224 370 SELEE-AREA-------------VEDRREEIEELEEEIEELRERFGDAPVDL----GNAEDFLEELREERDELREREAE- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 800 qhskamLSGQLRASEQKLRSTEaRLLEK------TQELRDLETQQALQRDRQKevqrlqecIAELSQQLGTSEQAQRLME 873
Cdd:PRK02224 431 ------LEATLRTARERVEEAE-ALLEAgkcpecGQPVEGSPHVETIEEDRER--------VEELEAELEDLEEEVEEVE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 874 KKLKRNYTllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQvhklEEELEAREASIRQ 953
Cdd:PRK02224 496 ERLERAED--LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----REAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 954 LAQHVQSLHDERDLIKHQFQELmERVATSDGDVAELQ---EKLRGKEVDYQNLE-HSHHRVSVQLQSVRTLLREKE---- 1025
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEdeiERLREKREALAELNdERRERLAEKRERKRELEAEFDeari 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907081936 1026 EELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
730-1041 |
5.60e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 730 ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQtrlgNAAAELAIKEQALAKLKGELKMEQGKVREQLEEwqhskamLSGQ 809
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELN----EELKELAEKRDELNAQVKELREEAQELREKRDE-------LNEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 810 LRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTS----EQAQRLMEK--KLKRNYTLL 883
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvlspEEEKELVEKikELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 884 LESCEQEKQallqnLKEVEDKASAYEDQLQGHVQQVEALQKEklsetckgSEQVHKleeeleareaSIRQLAQHVQSLHD 963
Cdd:COG1340 153 KKALEKNEK-----LKELRAELKELRKEAEEIHKKIKELAEE--------AQELHE----------EMIELYKEADELRK 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081936 964 ERDLIKHQFQELMERvatsdgdVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRtllreKEEELKHIKETHERVLEK 1041
Cdd:COG1340 210 EADELHKEIVEAQEK-------ADELHEEIIELQKELRELRKELKKLRKKQRALK-----REKEKEELEEKAEEIFEK 275
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
715-1071 |
5.82e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 715 NQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGElkmEQGKvRE 794
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSY-KQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 795 QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQ----ALQRDRQKEVQRLQECIAELSQQLGTSEQAQR 870
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 871 LMEKKLKrnytLLLESCEQEKQALLQNLKEVEDKASAYeDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREAS 950
Cdd:TIGR04523 465 SLETQLK----VLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 951 IRQLAQHVQSLHDE--RDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEEL 1028
Cdd:TIGR04523 540 ISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907081936 1029 KHIKETHERVLEKKDqDLNEALVKMIALGSSLEETEIKLQEKE 1071
Cdd:TIGR04523 620 EKAKKENEKLSSIIK-NIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
614-1069 |
6.29e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 614 QRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLE-KELEQSQKEASDLLEQNRLLQDQLRVALGREQSARE 692
Cdd:pfam07111 146 QRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEaKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 693 gYVLQTEVATSPSGAWqrlhrvnqdlqsELEaqcrRQELItQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELA 772
Cdd:pfam07111 226 -YVGEQVPPEVHSQTW------------ELE----RQELL-DTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 773 IKEQALAKLKGELKMeqgKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQA-----LQR---DR 844
Cdd:pfam07111 288 RKIQPSDSLEPEFPK---KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSqeqaiLQRalqDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 845 QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLL------LESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQ 918
Cdd:pfam07111 365 AAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLkfvvnaMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRK 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 919 V---EALQKEKLS------ETCKGSEqvhKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERvATSDGDVAEL 989
Cdd:pfam07111 445 VhtiKGLMARKVAlaqlrqESCPPPP---PAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGR-AREQGEAERQ 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 990 Q--EKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKM-IALGSSLEETEIK 1066
Cdd:pfam07111 521 QlsEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVeTRLREQLSDTKRR 600
|
...
gi 1907081936 1067 LQE 1069
Cdd:pfam07111 601 LNE 603
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
716-1072 |
6.72e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 716 QDLQSELEAQCRRQELITQQIQTLKHSYGEAKDA-------IRHHEAEIQTLQTRLGNAAAELAI----KEQALAK-LKG 783
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeLEQNNKKIKELEKQLNQLKSEISDlnnqKEQDWNKeLKS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 784 ELKMEQGKVRE---QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQ---KEVQRLQECIA 856
Cdd:TIGR04523 315 ELKNQEKKLEEiqnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEiEKLKKENQsykQEIKNLESQIN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 857 ELSQQLGTSEQAQRLME---KKLKRNYTLLLESCEQEKQALLQN---LKEVEDKASAYEDQLQGHVQQVEAlQKEKLSEt 930
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDeqiKKLQQEKELLEKEIERLKETIIKNnseIKDLTNQDSVKELIIKNLDNTRES-LETQLKV- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 931 ckgseqvhkleeeleaREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRV 1010
Cdd:TIGR04523 473 ----------------LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081936 1011 SVQLQSVRTLLREKEEELKhiKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1072
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
620-1086 |
8.35e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 620 ETTPLREEkQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQ-----SQKEASDLLEQNRLLQDQLRVALGREQSAREGY 694
Cdd:TIGR00618 401 ELDILQRE-QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 695 VLQTEVATSPSGAWQRLHRVnQDLQSELEAQCRRQELITQQIQTL------------KHSY-GEAKDAIRHHEAEIQTLQ 761
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPARQDIDNPgpltrrmqrgeqTYAQlETSEEDVYHQLTSERKQR 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 762 TRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSgqlraseqklRSTEARLLEKTQELRDLETQQALQ 841
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----------EAEDMLACEQHALLRKLQPEQDLQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 842 RDRQKEvqrlQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQN-LKEVEDKASAYEDQLQGHVQQVE 920
Cdd:TIGR00618 629 DVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLaLQKMQSEKEQLTYWKEMLAQCQT 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 921 ALQKEKLSETcKGSEQVHKLEEELEAREASIR-QLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVD 999
Cdd:TIGR00618 705 LLRELETHIE-EYDREFNEIENASSSLGSDLAaREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1000 YQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLRRFVS 1079
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
....*..
gi 1907081936 1080 DSPKDAK 1086
Cdd:TIGR00618 864 LTQEQAK 870
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1900-2130 |
8.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1900 LAPGPSEPRAVPAAKDEAEsMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQRDFESLKATcERGFAAMEeth 1979
Cdd:COG4942 10 LLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKE--EKALLKQLAALERRIAALARRIRAL-EQELAALE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1980 qKKIEDLQRQH---QRELEKLREEKDRLLA--------EETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEA 2048
Cdd:COG4942 83 -AELAELEKEIaelRAELEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2049 LRR------QYLEELQSVQRELE----VLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEIT 2118
Cdd:COG4942 162 LAAlraeleAERAELEALLAELEeeraALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|..
gi 1907081936 2119 RLRTLLTGDGGG 2130
Cdd:COG4942 242 RTPAAGFAALKG 253
|
|
| PH_DOCK-D |
cd13267 |
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ... |
48-145 |
8.80e-05 |
|
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270087 Cd Length: 126 Bit Score: 44.24 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 48 GWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHG----LLRYALDEMPTTlPQGTINMNQCTDVVDGEARTGQKFSLCILT 123
Cdd:cd13267 10 GYLYKGPENSSDSFISLAMKSFKRRFFHLKQLVdgsyILEFYKDEKKKE-AKGTIFLDSCTGVVQNSKRRKFCFELRMQD 88
|
90 100
....*....|....*....|..
gi 1907081936 124 PdKEHFIRAETKEIISGWLEML 145
Cdd:cd13267 89 K-KSYVLAAESEAEMDEWISKL 109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1923-2121 |
1.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1923 LRERIQELEAQMGVMREELghKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQhqreLEKLREEKD 2002
Cdd:COG3206 173 ARKALEFLEEQLPELRKEL--EEAEAALEEFRQKNG----------LVDLSEEAKLLLQQLSELESQ----LAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2003 RLLAEETAATiSAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEE---LQSVQRELEVLSEQYSQkclENA 2079
Cdd:COG3206 237 EAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQ---EAQ 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081936 2080 HLAQALEAERQALRQCQRE-NQELNAHNQELN--NRLAAEITRLR 2121
Cdd:COG3206 313 RILASLEAELEALQAREASlQAQLAQLEARLAelPELEAELRRLE 357
|
|
| PH_TBC1D2A |
cd01265 |
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ... |
67-145 |
1.12e-04 |
|
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269966 Cd Length: 102 Bit Score: 43.47 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081936 67 RKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQkFSlcILTPDKEHFIRAETKEIISGWLEML 145
Cdd:cd01265 17 KGWKRRWFVLDESKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAEPGQ-FE--IHTPGRVHILKASTRQAMLYWLQAL 92
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-930 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 716 QDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLkgelkmeqgkvREQ 795
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER-----------REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 796 LEEWQHSKAMLSGQLRASEQKLRSTE-ARLLEKTQELRDL-ETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLME 873
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 874 KKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSET 930
Cdd:COG3883 168 AAKAE-----LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
832-1080 |
1.35e-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: 47.36 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 832 RDLETQQALqRDRQKEVQRLQECIAELSQQLGT----SEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASA 907
Cdd:TIGR02168 173 RRKETERKL-ERTRENLDRLEDILNELERQLKSlerqAEKAERYKELKAELR--------ELELALLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 908 YEDQLQGHVQQVEALQKEKlsetckgseqvhkleeelEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVA 987
Cdd:TIGR02168 244 LQEELKEAEEELEELTAEL------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 988 ELQEKLRgkevdyqNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHErVLEKKDQDLNEALVKMIALgssLEETEIKL 1067
Cdd:TIGR02168 306 ILRERLA-------NLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAE---LEELESRL 374
|
250
....*....|...
gi 1907081936 1068 QEKEECLRRFVSD 1080
Cdd:TIGR02168 375 EELEEQLETLRSK 387
|
|
| PH_AtPH1 |
cd13276 |
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ... |
67-142 |
1.39e-04 |
|
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270095 Cd Length: 106 Bit Score: 43.07 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 67 RKWQRRFFILYEHGLLRY-ALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWL 142
Cdd:cd13276 13 KTWRRRWFVLKQGKLFWFkEPDVTPYSKPRGVIDLSKCLTVKSAEDATNKENAFELSTPEETFYFIADNEKEKEEWI 89
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1918-2183 |
1.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1918 ESMSGLRERIQELEAQMGVMREELGH------KELEGDVAALQEKYqRDFESLKATCERGFAAMEEtHQKKIEDLQRQHQ 1991
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRVKEKI-GELEAEIASLERSIAEKER-ELEDAEERLAKLE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1992 RELEKLREEKDRL---LAEETAATISAIEAMKNAHREEMEReleksqRSQISSINSDIEALRR---QYLEELQSVQRELE 2065
Cdd:TIGR02169 329 AEIDKLLAEIEELereIEEERKRRDKLTEEYAELKEELEDL------RAELEEVDKEFAETRDelkDYREKLEKLKREIN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2066 VLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTlltgdgggestglpLTQGKDAYE 2145
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ--------------LAADLSKYE 468
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907081936 2146 LEvlLRVKESEIQYLKQEISSLKDELQTALRDKKYASD 2183
Cdd:TIGR02169 469 QE--LYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1925-2101 |
1.55e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1925 ERIQELEA-QMGVMRE-ELGHKELEG--DVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKLREE 2000
Cdd:pfam17380 375 SRMRELERlQMERQQKnERVRQELEAarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2001 KdrLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISS---INSDIEALRRQYLEELQS---VQRELE-----VLSE 2069
Cdd:pfam17380 455 E--QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkiLEKELEERKQAMIEEERKrklLEKEMEerqkaIYEE 532
|
170 180 190
....*....|....*....|....*....|..
gi 1907081936 2070 QYSQKCLENAHLAQALEAERQALRQCQRENQE 2101
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
815-1018 |
1.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 815 QKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQ-QLGTSEQAQRLMEKKLKRNyTLLLESCEQEKQA 893
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL-RAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 894 LLQNLKEVEDKASAYEDQLQGH-VQQVEALQKEklsetckgseqVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQF 972
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNgGDRLEQLERE-----------IERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081936 973 QEL----MERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVR 1018
Cdd:COG4913 383 AALraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1912-2069 |
2.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1912 AAKDEAES-MSGLRERIQELEAQM---GVMREElghkELEGDVAALQEKY---QRDFESLKATCER-GFAAmeETHQKKI 1983
Cdd:COG4913 309 AELERLEArLDALREELDELEAQIrgnGGDRLE----QLEREIERLERELeerERRRARLEALLAAlGLPL--PASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1984 EDLQRQHQRELEKLREEKDRLLAEETAAtISAIEAMKNAHREeMERELEkSQRSQISSINSDIEALRRQYLEELQSVQRE 2063
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEA-EAALRDLRRELRE-LEAEIA-SLERRKSNIPARLLALRDALAEALGLDEAE 459
|
....*.
gi 1907081936 2064 LEVLSE 2069
Cdd:COG4913 460 LPFVGE 465
|
|
| PH_3BP2 |
cd13308 |
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ... |
66-145 |
2.15e-04 |
|
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270118 Cd Length: 113 Bit Score: 42.78 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 66 SRKWQRRFFILYEHGLLrYALDEMPTTlPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEH---FIRAETKEIISGWL 142
Cdd:cd13308 25 LQNWQLRYVIIHQGCVY-YYKNDQSAK-PKGVFSLNGYNRRAAEERTSKLKFVFKIIHLSPDHrtwYFAAKSEDEMSEWM 102
|
...
gi 1907081936 143 EML 145
Cdd:cd13308 103 EYI 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1713-2117 |
2.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1713 EYEKELRFYKKACQEAKGASGQKRAQAVGALKEE---YEELlhKQKSEYQKVITLIEKENTELKAKVSQMdhqqRCLQEA 1789
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkADEA--KKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1790 ENKHSESMFALQGRYEEEIRcMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRElqavh 1869
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----- 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1870 QEELRALQEHYIwslrgalslyqpshpdsslapgpsepravpaakdeaesmsglrERIQELEAQMGVMREELGHKELEGD 1949
Cdd:PTZ00121 1583 AEEAKKAEEARI-------------------------------------------EEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1950 VAALQEKYQrdfESLKATCERgFAAMEETHQKKIEDLQRQHqrELEKLREEKDRLLAEETAATISAIEAMKNAHREEMER 2029
Cdd:PTZ00121 1620 IKAEELKKA---EEEKKKVEQ-LKKKEAEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2030 ELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQEL 2109
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
....*...
gi 1907081936 2110 NNRLAAEI 2117
Cdd:PTZ00121 1774 RKEKEAVI 1781
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1806-2218 |
2.52e-04 |
|
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: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1806 EEIRCMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEHyIWSLR 1885
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELR-LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGE-LSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1886 GALSLYQpSHPDSSlapgpsEPRAVPAAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQRDFESLK 1965
Cdd:pfam12128 315 AAVAKDR-SELEAL------EDQHGAFLDADIETAAADQEQLPSWQSELENLEER--LKALTGKHQDVTAKYNRRRSKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1966 ATCERGFAAMEEthqkkiedlqrqhqrELEKLREEKDRLLAEETAatisAIEAMKNAHREEME------RELEKSQRSQI 2039
Cdd:pfam12128 386 EQNNRDIAGIKD---------------KLAKIREARDRQLAVAED----DLQALESELREQLEagklefNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2040 SSIN---------SDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELN 2110
Cdd:pfam12128 447 GELKlrlnqatatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2111 NRLAAEITRLRTLLTGDGGG--ESTG----------------LPLTQGKDAYEL-EVLLRVKESEIQ---YLKQEISSLK 2168
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPDweQSIGkvispellhrtdldpeVWDGSVGGELNLyGVKLDLKRIDVPewaASEEELRERL 606
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907081936 2169 DELQTALRDkkyASDKYKDIYTELSIAKA---KADCDISRLKEQLKAATEALG 2218
Cdd:pfam12128 607 DKAEEALQS---AREKQAAAEEQLVQANGeleKASREETFARTALKNARLDLR 656
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-884 |
2.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 710 RLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKE--QALAKLKGELKM 787
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 788 EQGKVRE------QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQE-----LRDLETQQALQRDRQKEVQRLQECIA 856
Cdd:COG4717 144 LPERLEEleerleELRELEEELEELEAELAELQEELEELLEQLSLATEEelqdlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 1907081936 857 ELSQQLGTSEQAQRL--MEKKLKRNYTLLL 884
Cdd:COG4717 224 ELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
709-1074 |
2.73e-04 |
|
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: 46.58 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNQDLQSELEAQCRRQELITQQIQTLK----------HSYGEAKDAIRHHEAEIQTLQtrlgnaAAELAIKEQAL 778
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimeRFQMELKDVERKIAQQAAKLQ------GSDLDRTVQQV 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 779 AKLKGELKMEQGKVREQLEEWQHskamLSGQLRASEQKLRSTEARL-LEKTQELRDLETQQALQRDRQKEVQRLQECIAE 857
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRK----LIQDQQEQIQHLKSKTNELkSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 858 LSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQAL--LQNLKEVEDKASAYEDQLQGHVQQ-VEALQKEKLSETCKGS 934
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdkVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVN 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 935 EQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQF---------QELMERVATSDGDVAELQekLRGKEVDYQNLEH 1005
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlrkrenelKEVEEELKQHLKEMGQMQ--VLQMKQEHQKLEE 1061
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081936 1006 SHHRVSVQLQSVRTLLREKEEELKHIKethERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECL 1074
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFK---KELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTL 1127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1742-2171 |
2.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1742 ALKEEYEELLhKQKSEYQKVITLIEKENTELKAKVSQmdhqqrcLQEAENKHSESMFALQGRYE--EEIRCMVEQLSHTE 1819
Cdd:PRK03918 176 RRIERLEKFI-KRTENIEELIKEKEKELEEVLREINE-------ISSELPELREELEKLEKEVKelEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1820 NTLQAErsrvLSQLDASVKDRQAMEQHHVQQMKMLEDrfqlKVRELqavhqEELRALQEHYIwSLRGALSLY--QPSHPD 1897
Cdd:PRK03918 248 ESLEGS----KRKLEEKIRELEERIEELKKEIEELEE----KVKEL-----KELKEKAEEYI-KLSEFYEEYldELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1898 SSLAPGPSEPRAVPAAKDEAESMSglrERIQELEAQMGVMREELGhkELEGDVAALQEKYQRDFESLKATCERGFAAMEE 1977
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRLE--ELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1978 ThQKKIEDLQRQH---QRELEKLREEKDRLLAEEtAATISAIEAMKNAHR----------EEMERELEKSQRSQISSINS 2044
Cdd:PRK03918 389 L-EKELEELEKAKeeiEEEISKITARIGELKKEI-KELKKAIEELKKAKGkcpvcgreltEEHRKELLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2045 DIEALRRQyLEELQSVQRELEVLSEQYSQkclenahlaqaLEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLL 2124
Cdd:PRK03918 467 ELKEIEEK-ERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907081936 2125 TGDGGgESTGLpLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDEL 2171
Cdd:PRK03918 535 IKLKG-EIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
639-1069 |
3.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 639 LEDRSERLSTheltslLEKELEQSQKEASDLLEQNRLLQD--QLRVALGREQSAREGYVLQtevatspsgawqrlhrvnq 716
Cdd:PRK03918 333 LEEKEERLEE------LKKKLKELEKRLEELEERHELYEEakAKKEELERLKKRLTGLTPE------------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 717 DLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNA---AAELAikEQALAKLKGELKMEQGKVR 793
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcGRELT--EEHRKELLEEYTAELKRIE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 794 EQLEEWQHSKAMLSGQLRASEQKLR--STEARLLEKTQELRDLETQqaLQRDRQKEVQRLQECIAELSQQLGTSEQAQRL 871
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 872 MEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEalqkEKLSETCKGSEQVHKLEEELEAREASI 951
Cdd:PRK03918 544 LKKELEK-----LEELKKKLAELEKKLDELEEELAELLKELEELGFESV----EELEERLKELEPFYNEYLELKDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 952 RQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAEL-----QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEE 1026
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907081936 1027 ELKHIKETHERVLEKKDQ--DLNEALVKMIALGSSLEETEIKLQE 1069
Cdd:PRK03918 695 TLEKLKEELEEREKAKKEleKLEKALERVEELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-913 |
3.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 611 EIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEK--ELEQSQKEASDLLEQNRLLQDQLRVALGREQ 688
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 689 SAREGyvLQTEVATSPsgaWQRLhrvnQDLQSELEAQCRRQELITQQIQ------TLKHSYgeAKDAIRHHEAEIQTLQT 762
Cdd:TIGR02169 779 EALND--LEARLSHSR---IPEI----QAELSKLEEEVSRIEARLREIEqklnrlTLEKEY--LEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 763 RLGNAAAELAIKEQALAKLKGELKMEQGKVRE---QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQA 839
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 840 LQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQ 913
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE-----IRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1778-2196 |
4.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1778 QMDHQQRCLQEAENKHSESMFAlqgRYEEEIRCMVEQLSHTeNTLQAERSRVLSQldaSVKDRQAmeqhHVQQMKMLEDR 1857
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLE---EYSHQVKDLQRRLNES-NELHEKQKFYLRQ---SVIDLQT----KLQEMQMERDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1858 FqLKVRELQAVHQEELRALQEHYIWSLRGALSLYQPSHPDSSLAPGP------------SEPRAVPAAKDEAESmsglrE 1925
Cdd:pfam15921 129 M-ADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkmmlshegvlQEIRSILVDFEEASG-----K 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1926 RIQELEAQMGVMREELGH------KELEGDVAALQEK---YQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEK 1996
Cdd:pfam15921 203 KIYEHDSMSTMHFRSLGSaiskilRELDTEISYLKGRifpVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1997 LREEKdrllaeetaatiSAIEAMKNAHREEME--RELEKSQRSQISSINSDIEALRRQYLEELQSVQRELE-VLSEQYSQ 2073
Cdd:pfam15921 283 LTEKA------------SSARSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdKIEELEKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2074 KCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNR---LAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVll 2150
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRekeLSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV-- 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907081936 2151 RVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAK 2196
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1919-2276 |
4.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1919 SMSGLRERIQELEAQMGVMREELghKELEGDVAALQE------------KYQRDFESLKATCERGFAAMEETH---QKKI 1983
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEI--EELEEKVKELKElkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEIngiEERI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1984 EDLQRQHQR--ELEKLREEKDRLLA--EETAATISAIEAMKnahrEEMERELEKSQRSQISSINSDIEALRRQYLEelqs 2059
Cdd:PRK03918 331 KELEEKEERleELKKKLKELEKRLEelEERHELYEEAKAKK----EELERLKKRLTGLTPEKLEKELEELEKAKEE---- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2060 VQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNA-HNQELNNRLAAEITRLRTLLTGDGGGESTGLplt 2138
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEeHRKELLEEYTAELKRIEKELKEIEEKERKLR--- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2139 qgKDAYELEVLLRvKESEIQYLKQ---EISSLKDELqtalrdKKYASDKYKDIYTELSIAKAKAD---CDISRLKEQLKA 2212
Cdd:PRK03918 480 --KELRELEKVLK-KESELIKLKElaeQLKELEEKL------KKYNLEELEKKAEEYEKLKEKLIklkGEIKSLKKELEK 550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 2213 ATEALGEKSpegttvsgydimKSKSNPDFLKKDRSCVTRQLRNIRSKSLKEgltVQERLKLFES 2276
Cdd:PRK03918 551 LEELKKKLA------------ELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELEP 599
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
393-458 |
4.41e-04 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 41.77 E-value: 4.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 393 LTKQYEDGQAADLDGEINLSTC---YDVTEYPVQRNYGFQIHTKEGE-FTLSAMTSGIRRNWIQTIMKHV 458
Cdd:smart00233 32 YYKSKKDKKSYKPKGSIDLSGCtvrEAPDPDSSKKPHCFEIKTSDRKtLLLQAESEEEREKWVEALRKAI 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1992-2259 |
4.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1992 RELEKLREEKDRLLAEEtaatiSAIEAMKnahrEEMERELEKSQRsQISSINSDIEALRRQyLEELQSVQRELEVLSEQY 2071
Cdd:PRK03918 172 KEIKRRIERLEKFIKRT-----ENIEELI----KEKEKELEEVLR-EINEISSELPELREE-LEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2072 SQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRlAAEITRLRTLltgdgggestglpltqgKDAY-ELEVLL 2150
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEK-----------------AEEYiKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2151 RVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIyTELSIAKAKADCDISRLKEQLKAATEA---LGEKSPEGTTV 2227
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHELYEEAkakKEELERLKKRL 381
|
250 260 270
....*....|....*....|....*....|..
gi 1907081936 2228 SGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSK 2259
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
771-1027 |
5.19e-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: 44.75 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 771 LAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQrdrQKEVQR 850
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 851 LQECIAELSQQLGTSEQ--AQRL--MEKKLKRNYTLLLESCEqekqallqNLKEVEDKASAYEDQLQGHVQQVEALqkek 926
Cdd:COG4942 88 LEKEIAELRAELEAQKEelAELLraLYRLGRQPPLALLLSPE--------DFLDAVRRLQYLKYLAPARREQAEEL---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 927 lsetckgseqvhklEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHS 1006
Cdd:COG4942 156 --------------RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260
....*....|....*....|.
gi 1907081936 1007 HHRVSVQLQSVRTLLREKEEE 1027
Cdd:COG4942 222 AEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1724-2208 |
5.24e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1724 ACQEAKGASGQKRAQAVGALKEEYEELLHKQKsEYQKVITLIEKENTELKAKVSqmdhqqrclqEAENKHSESMFALqgr 1803
Cdd:pfam05483 198 AFEELRVQAENARLEMHFKLKEDHEKIQHLEE-EYKKEINDKEKQVSLLLIQIT----------EKENKMKDLTFLL--- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1804 yeEEIRCMVEQLSHtENTLQAERSRVLSQ----LDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEH 1879
Cdd:pfam05483 264 --EESRDKANQLEE-KTKLQDENLKELIEkkdhLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1880 YIWSLRGALSLYQPSHPDSSLAPG-PSEPRAVPAAKD-------EAESMSGLRERIQELEAQMGVMREELgHKELEGDVA 1951
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDqlkiitmELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1952 ALQEKYQRD--FESLKATcERGFAAMEETHQKKIEDLQRQ----------HQRELEKLREE--KDRLLAEETAATISAIE 2017
Cdd:pfam05483 420 LLDEKKQFEkiAEELKGK-EQELIFLLQAREKEIHDLEIQltaiktseehYLKEVEDLKTEleKEKLKNIELTAHCDKLL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2018 AMKNAHREE---MERELEKSQRSQISSINSDIEALRR-QYLEELQSVQR-ELEVLSEQYSQ-----KCLENAHLAQALEA 2087
Cdd:pfam05483 499 LENKELTQEasdMTLELKKHQEDIINCKKQEERMLKQiENLEEKEMNLRdELESVREEFIQkgdevKCKLDKSEENARSI 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2088 ERQALRQCQRENQELNAHNQ-----ELNNRLAAEITRLRTLLTGDGGGESTGLpltqgkDAYELEVllRVKESEIQYLKQ 2162
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNlkkqiENKNKNIEELHQENKALKKKGSAENKQL------NAYEIKV--NKLELELASAKQ 650
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1907081936 2163 EISSLKDELQTALRDKKYASDKykdIYTELSIAKAKADCDISRLKE 2208
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEK---LLEEVEKAKAIADEAVKLQKE 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
655-1050 |
5.96e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSA-------REGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCR 727
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqlrariEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 728 RQ-ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGN-----AAAELAIKEQALAKLKGELKMEQGKVREQLEEWQH 801
Cdd:TIGR00618 307 QQaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlqtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 802 SKAMLSGQLRASEQ---KLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKR 878
Cdd:TIGR00618 387 QKTTLTQKLQSLCKeldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 879 NYTLLLEScEQEKQALLQNLKEVEDKASAYEDQLQG------------HVQQVEALQKEKLSETCKGSEQVHKLEEELEA 946
Cdd:TIGR00618 467 SLKEREQQ-LQTKEQIHLQETRKKAVVLARLLELQEepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 947 REASIRQ-LAQHVQSLHDERDLIKHQFQELmervATSDGDVAELQEKLRGKEVDYQNL--EHSHHRVSVQLQSVRTLLRE 1023
Cdd:TIGR00618 546 DVYHQLTsERKQRASLKEQMQEIQQSFSIL----TQCDNRSKEDIPNLQNITVRLQDLteKLSEAEDMLACEQHALLRKL 621
|
410 420
....*....|....*....|....*..
gi 1907081936 1024 KEEELKHIKETHERVLEKKDQDLNEAL 1050
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1914-2094 |
5.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1914 KDEAESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCERgfaameethqkkIEDLQRQHQrE 1993
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER------------LEELEERLE-E 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1994 LEKLREEKDRLLAEetaatisaiEAMKNAHREEMERELEKSQRSQISSINSDIEALR---RQYLEELQSVQRELEVLSEQ 2070
Cdd:COG4717 158 LRELEEELEELEAE---------LAELQEELEELLEQLSLATEEELQDLAEELEELQqrlAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....
gi 1907081936 2071 YSQkcLENAHLAQALEAERQALRQ 2094
Cdd:COG4717 229 LEQ--LENELEAAALEERLKEARL 250
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1974-2126 |
7.57e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1974 AMEETHQKKIEDLQRQHQRELEKLREEKDRL--LAEETAATISAIEAMKNAHREEM--ERELEKSQRSQISSINSDIEAL 2049
Cdd:PRK09039 70 SLERQGNQDLQDSVANLRASLSAAEAERSRLqaLLAELAGAGAAAEGRAGELAQELdsEKQVSARALAQVELLNQQIAAL 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081936 2050 RRQyleeLQSVQRELEVlSEQYSQkclenahlaqalEAERQALRQCQRENQELNAHNQELnNRLAAE-ITRLRTLLTG 2126
Cdd:PRK09039 150 RRQ----LAALEAALDA-SEKRDR------------ESQAKIADLGRRLNVALAQRVQEL-NRYRSEfFGRLREILGD 209
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1713-2004 |
9.26e-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: 44.66 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1713 EYEKELRFYKKACQEAKGASGQKRaQAVGALKEEYEELLHKQKSEYQKvITLIEKENTELKAKVSQMDHQQRCLQEAENK 1792
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELS-RQISALRKDLARLEAEVEQLEER-IAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1793 HSESMFALQGRYEEeircMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVREL--QAVHQ 1870
Cdd:TIGR02168 780 AEAEIEELEAQIEQ----LKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeeLSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1871 EELRALQEHYiWSLRGALSlyqpSHPDSSLAPGPSEPRAVPAAKDEAESMSG----LRERIQELEAQMGVMREELGH--- 1943
Cdd:TIGR02168 855 ESLAAEIEEL-EELIEELE----SELEALLNERASLEEALALLRSELEELSEelreLESKRSELRRELEELREKLAQlel 929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 1944 --KELEGDVAALQEK----YQRDFEslkatcergfaaMEETHQKKIEDLQRQHQRELEKLREEKDRL 2004
Cdd:TIGR02168 930 rlEGLEVRIDNLQERlseeYSLTLE------------EAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1912-2208 |
9.74e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1912 AAKDEAESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCE-----RGFAAMEETHQKKIEDL 1986
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeskRETETGIQNLTAEIEQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1987 QRQHQRELEKLREEKDRLLAEETAATisaieamknahREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEV 2066
Cdd:COG5185 349 QESLTENLEAIKEEIENIVGEVELSK-----------SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2067 LSEQysqkclenahlaqaLEAERQALRQCQRENQElnahNQELNNRLAAEITRLRTLLTGDGggeSTGLPLTQGKDAYEL 2146
Cdd:COG5185 418 ADRQ--------------IEELQRQIEQATSSNEE----VSKLLNELISELNKVMREADEES---QSRLEEAYDEINRSV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 2147 EVLLRVKESEIQYLKQEISSLKDELQT--ALRDKKYASDKYKDIYTELSIAKAKADCDISRLKE 2208
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKlrAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
711-936 |
9.91e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 711 LHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKlkgeLKMEQG 790
Cdd:PHA02562 190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK----LNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 791 KVREQLEEWQHSKAMLS--GQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQKEVQRLQEcIAELSQQLgtseq 867
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSlEKLDTAIDELEEIMDE-FNEQSKKL----- 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081936 868 aqrlmeKKLKRNYtlllESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKE--KLSETCKGSEQ 936
Cdd:PHA02562 340 ------LELKNKI----STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEldKIVKTKSELVK 400
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1617-2094 |
1.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1617 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLPPTEPLGGCQRLLRMSQHlSYESCLEGLGQYSSLLVQd 1696
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE-RLEELEERLEELRELEEE- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1697 aiiqaqvcyaacriRLEYEKELRFYKKACQEAKGASGQKRAQAVGALKEEYEELlHKQKSEYQKVITLIEKENTELKAKV 1776
Cdd:COG4717 165 --------------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL-QQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1777 SQMDHQQRCLQEAENKHSESMFALqgryeeeIRCMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLED 1856
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLL-------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1857 RFQlkvrelQAVHQEELRALQEHYIWSLRGALSLyqpshpdsslaPGPSEPRAVPAAKDEAESMSGLRERIQELEAQMgv 1936
Cdd:COG4717 303 EAE------ELQALPALEELEEEELEELLAALGL-----------PPDLSPEELLELLDRIEELQELLREAEELEEEL-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1937 mreelghkelegDVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQR--QHQRELEKLREEKDRLLAEETAATIS 2014
Cdd:COG4717 364 ------------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2015 AIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQY-----LEELQSVQRELEVLSEQYSQKCLenahLAQALEAER 2089
Cdd:COG4717 432 EELEELEEELEELEEELEE-LREELAELEAELEQLEEDGelaelLQELEELKAELRELAEEWAALKL----ALELLEEAR 506
|
....*
gi 1907081936 2090 QALRQ 2094
Cdd:COG4717 507 EEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1912-2174 |
1.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1912 AAKDEAEsmsgLRERIQELEAQMGVMREELGHKELEGDVAALQ-----------EKYQRDFESLKATCERGFAAMEETHQ 1980
Cdd:PRK02224 197 EEKEEKD----LHERLNGLESELAELDEEIERYEEQREQARETrdeadevleehEERREELETLEAEIEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1981 KK--IEDLQRQHQRELEKLREEKDRLLAEE--TAATISAIEAMKN---AHREEMERELEKsQRSQISSINSDIEALRrqy 2053
Cdd:PRK02224 273 EReeLAEEVRDLRERLEELEEERDDLLAEAglDDADAEAVEARREeleDRDEELRDRLEE-CRVAAQAHNEEAESLR--- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2054 leelqsvqRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAaeitrlrtlltgdgggest 2133
Cdd:PRK02224 349 --------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG------------------- 401
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907081936 2134 GLPLTQGKDAYELEVLLrvkeSEIQYLKQEISSLKDELQTA 2174
Cdd:PRK02224 402 DAPVDLGNAEDFLEELR----EERDELREREAELEATLRTA 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1917-2117 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1917 AESMSGLRERIQELEAQMGVMR--------------EELGHKELEGDVAALQEKYQR------DFESLK---ATCERGFA 1973
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQerrealqrlaeyswDEIDVASAEREIAELEAELERldassdDLAALEeqlEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1974 AMEEtHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAI------------EAMKNAHREEMERELEKSQ---RSQ 2038
Cdd:COG4913 703 ELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelralleerfaAALGDAVERELRENLEERIdalRAR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2039 ISSINSDIEALRRQYLEE----LQSVQRELEVLSEqYSQKC--LENAHLAQALEAERQALRQCQRENQElnahnqELNNR 2112
Cdd:COG4913 782 LNRAEEELERAMRAFNREwpaeTADLDADLESLPE-YLALLdrLEEDGLPEYEERFKELLNENSIEFVA------DLLSK 854
|
....*
gi 1907081936 2113 LAAEI 2117
Cdd:COG4913 855 LRRAI 859
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
655-1074 |
1.11e-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: 44.34 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNrllQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQelITQ 734
Cdd:pfam15921 247 LEALKSESQNKIELLLQQH---QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ--LSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 735 QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQAlaklKGELKMEQGKVREQLEEwqhskamLSGQLRASE 814
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNLDDQLQK-------LLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 815 QKLRstearlLEKTQELR--DLETQQA-----LQR---DRQKEVQRLQ--------ECIAELSQQLGTSEQAQRLMEKkl 876
Cdd:pfam15921 391 KELS------LEKEQNKRlwDRDTGNSitidhLRReldDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEK-- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 877 krnYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSE--QVHKLEEELEAREASIRQL 954
Cdd:pfam15921 463 ---VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 955 AQHVQSLHDERDLIKHQFQELMERVatsdgdvaelqEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLrEKE--------E 1026
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVI-----------EILRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEindrrlelQ 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907081936 1027 ELKHIKETHE---RVLEKKDQDLNEALVKMIALGSS-LEETEIKLQEKEECL 1074
Cdd:pfam15921 608 EFKILKDKKDakiRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLL 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
653-822 |
1.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 653 SLLEKELEQSQKEAS----DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRR 728
Cdd:COG4942 79 AALEAELAELEKEIAelraELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 729 QELITQQIQTLKhsygEAKDAIRHHEAEIQTLQTRLgnaAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSG 808
Cdd:COG4942 159 LAELAALRAELE----AERAELEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....
gi 1907081936 809 QLRASEQKLRSTEA 822
Cdd:COG4942 232 LEAEAAAAAERTPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
620-1035 |
1.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 620 ETTPLREEKQVPIAPLH-----LSLE-DRSERLSTHELTSL-----LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQ 688
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHkrekeLSLEkEQNKRLWDRDTGNSitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 689 SAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGnaa 768
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD--- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 769 aelaIKEQALAKLKGE---------------LKM-EQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLlEKTQELR 832
Cdd:pfam15921 528 ----LKLQELQHLKNEgdhlrnvqtecealkLQMaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEINDR 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 833 DLETQQ--ALQRDRQKEVQRLQECIAEL-----------SQQLGT-----SEQAQRLMEKKLKRNYtllLESCEQEKQAL 894
Cdd:pfam15921 603 RLELQEfkILKDKKDAKIRELEARVSDLelekvklvnagSERLRAvkdikQERDQLLNEVKTSRNE---LNSLSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 895 LQNLKEVEDKASAYEDQLQGHVQ--QVEALQKEKLSETCKGSE------------QVHKLEEELEAREASIRQLAQHVQS 960
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKMQLKsaQSELEQTRNTLKSMEGSDghamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTN 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 961 LHDERDLIKHQFQEL---MERVATSDGDVAELQEKLRGKEVDYQ----NLEHSHHRVSVQLQSVRTLLREKEEELKHIKE 1033
Cdd:pfam15921 760 ANKEKHFLKEEKNKLsqeLSTVATEKNKMAGELEVLRSQERRLKekvaNMEVALDKASLQFAECQDIIQRQEQESVRLKL 839
|
..
gi 1907081936 1034 TH 1035
Cdd:pfam15921 840 QH 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2033-2240 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2033 KSQRSQISSINSDIEALRrqylEELQSVQRELEVLSEQYSQKcleNAHLAQALEAERQALRQCQRENQELNAHNQELNNR 2112
Cdd:COG3883 19 QAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2113 LAA------EITRLRTLLTGDGGGE--------STGLPLTQG--KDAYELEVLLRVKESEIQYLKQEISSLKDELQTALR 2176
Cdd:COG3883 92 ARAlyrsggSVSYLDVLLGSESFSDfldrlsalSKIADADADllEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 2177 DKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPD 2240
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
604-1029 |
1.47e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 604 KTQNVHVEIEQRWHQVETT--PLREEKQVPIAPLHLSLEDRSERLstHELTSLLEKELEQSQKEASDLLEQNRLLQDQLR 681
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAfeELRVQAENARLEMHFKLKEDHEKI--QHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 682 VALGREQSAREGyVLQTEVATSpsgawqrlhrvnqdLQSE-LEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTL 760
Cdd:pfam05483 258 DLTFLLEESRDK-ANQLEEKTK--------------LQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 761 QTRLGNAAAELAIKEQALAKLKGELKMeqgkvreQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELR----DLET 836
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSF-------VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQkkssELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 837 QQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKklkrnytllLESCEQEKQALLQNL-KEVED---KASAYEDQL 912
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE---------LKGKEQELIFLLQAReKEIHDleiQLTAIKTSE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 913 QGHVQQVEALQKEKLSETCKGSEqvhkleeeleareasirqLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEK 992
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIE------------------LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907081936 993 LRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELK 1029
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
767-1042 |
1.50e-03 |
|
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: 43.80 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 767 AAAELAIKEQALAK---LKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRD 843
Cdd:TIGR00618 182 ALMEFAKKKSLHGKaelLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 844 RQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQ 923
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 924 KEKLSETCKGSEQVH------------KLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSD-------- 983
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHirdahevatsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtsafrd 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081936 984 --GDVAEL-------QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKK 1042
Cdd:TIGR00618 422 lqGQLAHAkkqqelqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1736-2198 |
1.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1736 RAQAVGALKEEYEELLHKQKSEYQKVITLIEKENTELKAKVSQMDHQQRcLQEAENKHSESMFALQGRYEE---EIRCMV 1812
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEElreELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1813 EQLSHTENTLQAER-SRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQlKVRELQAVHQEELRALQEHYIWSLRGALSLY 1891
Cdd:COG4717 123 KLLQLLPLYQELEAlEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1892 QpshpdsslapgpsepravpAAKDEAESmsgLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCER- 1970
Cdd:COG4717 202 E-------------------ELQQRLAE---LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1971 GFAAMEETHQKKIEDLQRQHQ-----RELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSD 2045
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVLFlvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2046 IEALRRqyLEELQSVQRELEVLSEQYSQKCLE---NAHLAQALEAERQALRQCQRENQELnahnQELNNRLAAEITRLRT 2122
Cdd:COG4717 340 LELLDR--IEELQELLREAEELEEELQLEELEqeiAALLAEAGVEDEEELRAALEQAEEY----QELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 2123 LLTGDGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYAsdkykDIYTELSIAKAK 2198
Cdd:COG4717 414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-----ELLQELEELKAE 484
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
711-1076 |
1.57e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 711 LHRVNQDLQSELEAQCRRQELITQQIQT--------------LKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAE------ 770
Cdd:pfam10174 245 LERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevykshskfMKNKIDQLKQELSKKESELLALQTKLETLTNQnsdckq 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 771 --------LAIKEQALAKLKGE-----LKMEQ-----GKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELR 832
Cdd:pfam10174 325 hievlkesLTAKEQRAAILQTEvdalrLRLEEkesflNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 833 DLETQqalQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDkasaYEDQL 912
Cdd:pfam10174 405 NLQEQ---LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELES----LKKEN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 913 QGHVQQVEALQKEKLSETCKGS---EQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDvAEL 989
Cdd:pfam10174 478 KDLKEKVSALQPELTEKESSLIdlkEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTN-PEI 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 990 QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEElKHIKETHERVLEK------KDQDLNEALVKMialgSSLEET 1063
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAELESltlrqmKEQNKKVANIKH----GQQEMK 631
|
410
....*....|...
gi 1907081936 1064 EIKLQEKEECLRR 1076
Cdd:pfam10174 632 KKGAQLLEEARRR 644
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1917-2086 |
1.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1917 AESMSGLRERIQELEAQMGVMREELghKELEGDVAALQEKYQRDFESLKATCErgfAAMEETHQKKIEDLQRQHQRELEK 1996
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAEL--AEAEARLAALRAQLGSGPDALPELLQ---SPVIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1997 LREEKDRL--LAEETAATISAIEAMKNAHREEMERELEkSQRSQISSINSDIEALRRQYLE------ELQSVQRELEVLS 2068
Cdd:COG3206 286 YTPNHPDViaLRAQIAALRAQLQQEAQRILASLEAELE-ALQAREASLQAQLAQLEARLAElpeleaELRRLEREVEVAR 364
|
170 180
....*....|....*....|
gi 1907081936 2069 EQYSQ--KCLENAHLAQALE 2086
Cdd:COG3206 365 ELYESllQRLEEARLAEALT 384
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
715-1181 |
1.85e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 715 NQDLQSELEAQCRRQELITQQI----QTLKHSYGEAkdAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKmEQG 790
Cdd:COG5022 819 IIKLQKTIKREKKLRETEEVEFslkaEVLIQKFGRS--LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK-SIS 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 791 KVREQLEEWQHSKAMLSGQLRASEQ---KLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLgtseq 867
Cdd:COG5022 896 SLKLVNLELESEIIELKKSLSSDLIenlEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETS----- 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 868 aqrlmekklkrnytlllesceQEKQALLqnlkeveDKASAYEDQLQGHVQQVEALQKEkLSETCKGSEQVHKLEEELEAR 947
Cdd:COG5022 971 ---------------------EEYEDLL-------KKSTILVREGNKANSELKNFKKE-LAELSKQYGALQESTKQLKEL 1021
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 948 EASIRQLAQHVQSLHDERDlIKHQFQELMERVATSDGDVAELQEKLrgKEVDYQN-LEHSHHRVSVQLQSVRTLlrEKEE 1026
Cdd:COG5022 1022 PVEVAELQSASKIISSEST-ELSILKPLQKLKGLLLLENNQLQARY--KALKLRReNSLLDDKQLYQLESTENL--LKTI 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1027 ELKHIKETHERVLEKKdqdlnEALVKMIALGSSLEEteikLQEKEECLRRFVSDSPkDAKEPLSTTEPTEEGSGILPLGS 1106
Cdd:COG5022 1097 NVKDLEVTNRNLVKPA-----NVLQFIVAQMIKLNL----LQEISKFLSQLVNTLE-PVFQKLSVLQLELDGLFWEANLE 1166
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1107 VTRVFPGFpHSQPEDEDPSAGLGEEGSSGS-------------LSREENTILPKSADMPE--REG-HLQSTSKSDPGapI 1170
Cdd:COG5022 1167 ALPSPPPF-AALSEKRLYQSALYDEKSKLSssevndlkneliaLFSKIFSGWPRGDKLKKliSEGwVPTEYSTSLKG--F 1243
|
490
....*....|.
gi 1907081936 1171 KRPRIRFSTIQ 1181
Cdd:COG5022 1244 NNLNKKFDTPA 1254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1917-2102 |
1.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1917 AESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQekyQRDFESLKATCERgfaAMEETHQKkiedlQRQHQRELEK 1996
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR---REELEDRDEELRD---RLEECRVA-----AQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1997 LREEKDRLlaEETAATISAIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQY---LEELQSVQRELEVLSEQysq 2073
Cdd:PRK02224 347 LREDADDL--EERAEELREEAAELESELEEAREAVED-RREEIEELEEEIEELRERFgdaPVDLGNAEDFLEELREE--- 420
|
170 180 190
....*....|....*....|....*....|
gi 1907081936 2074 kcLENAHLAQA-LEAERQALRQCQRENQEL 2102
Cdd:PRK02224 421 --RDELREREAeLEATLRTARERVEEAEAL 448
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
655-918 |
2.55e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRvalgREQSAREGYVLQTEVATSpsgAWQRL-------HRVNQDLQSELEAQCR 727
Cdd:PRK10246 535 LEKEVKKLGEEGAALRGQLDALTKQLQ----RDESEAQSLRQEEQALTQ---QWQAVcaslnitLQPQDDIQPWLDAQEE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 728 RQELITQ--QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIK------EQA-LAKLKGELKMEQGKVREQ--L 796
Cdd:PRK10246 608 HERQLRLlsQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTlpqedeEASwLATRQQEAQSWQQRQNELtaL 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 797 EEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRD----LETQ-QALQRDRQKEVQRLQECIAELSQQLGTSEQAQR- 870
Cdd:PRK10246 688 QNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEqclsLHSQlQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQq 767
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907081936 871 ------LMEKKLKRnytlllesCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQ 918
Cdd:PRK10246 768 aflaalLDEETLTQ--------LEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
709-863 |
2.57e-03 |
|
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: 43.03 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 709 QRLHRVNQDLQSELEA-QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQtRLGNAAAELAIKEQALAKLKGELKM 787
Cdd:TIGR00618 725 NASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA-ELSHLAAEIQFFNRLREEDTHLLKT 803
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 788 EQGKVREQLEewqHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLG 863
Cdd:TIGR00618 804 LEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1726-2123 |
2.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1726 QEAKGASGQ-KRAQA-VGALKEEYEE------LLHKQKSEYQKVITLIEKENTELKAKVSqmDHQQRcLQEAENKhsesm 1797
Cdd:PRK04863 341 QTALRQQEKiERYQAdLEELEERLEEqnevveEADEQQEENEARAEAAEEEVDELKSQLA--DYQQA-LDVQQTR----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1798 fALQGRyeeeircmveqlshteNTLQA-ERSRVLSQLDA----SVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEE 1872
Cdd:PRK04863 413 -AIQYQ----------------QAVQAlERAKQLCGLPDltadNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1873 LRALQehyiwSLRgalslyqpshpdsSLAPGPSEPRAVPAAKD---EAESMSGLRERIQELEAQmgvmreelgHKELEGD 1949
Cdd:PRK04863 476 EQAYQ-----LVR-------------KIAGEVSRSEAWDVAREllrRLREQRHLAEQLQQLRMR---------LSELEQR 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1950 VAAlqekyQRDFESLKATCERGFAAMEEThQKKIEDLQRQHQRELEKLREEKDRLlaeetaatisaieamkNAHREEMER 2029
Cdd:PRK04863 529 LRQ-----QQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEA----------------RERRMALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2030 ELEKsqrsqissINSDIEALRRQYLEELQSvQRELEVLSEQY------SQKCLEnaHLAQALEAERQALR---QCQRENQ 2100
Cdd:PRK04863 587 QLEQ--------LQARIQRLAARAPAWLAA-QDALARLREQSgeefedSQDVTE--YMQQLLERERELTVerdELAARKQ 655
|
410 420
....*....|....*....|...
gi 1907081936 2101 ELNAHNQELNNRLAAEITRLRTL 2123
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNAL 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1987-2259 |
2.81e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1987 QRQHQRELEKLREEKDRLLAEEtAATISAIEAMKNaHREEMERELEKSQRsQISSINSDIEALrrqyLEELQSVQRELEV 2066
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKREL-SSLQSELRRIEN-RLDELSQELSDASR-KIGEIEKEIEQL----EQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2067 LSEQYSQkclenahLAQALEAERQALRQCQRENQELnahnQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYEL 2146
Cdd:TIGR02169 742 LEEDLSS-------LEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2147 EVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKadcdISRLKEQLKAATEALgekspegtt 2226
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAAL--------- 877
|
250 260 270
....*....|....*....|....*....|...
gi 1907081936 2227 vsgYDIMKSKSNpdfLKKDRSCVTRQLRNIRSK 2259
Cdd:TIGR02169 878 ---RDLESRLGD---LKKERDELEAQLRELERK 904
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
716-924 |
3.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 716 QDLQSELEAQCRRQELITQQ---IQTLKHSYgEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKG--------- 783
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDklvQQDLEQTL-ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdndeetret 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 784 -------ELKMEQGKVREQLEEWQHSKAMLSGQL--------RASEQkLRSTEARLLEKTQELRDLETQQALQRDRQKev 848
Cdd:PRK11281 118 lstlslrQLESRLAQTLDQLQNAQNDLAEYNSQLvslqtqpeRAQAA-LYANSQRLQQIRNLLKGGKVGGKALRPSQR-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 849 QRLQECIAELSQQ-------LGTSEQAQRLMEKklKRNYTLLLESCEQEKQALLQNLkeVEDKasaYEDQLQGHVQQVEA 921
Cdd:PRK11281 195 VLLQAEQALLNAQndlqrksLEGNTQLQDLLQK--QRDYLTARIQRLEHQLQLLQEA--INSK---RLTLSEKTVQEAQS 267
|
...
gi 1907081936 922 LQK 924
Cdd:PRK11281 268 QDE 270
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1980-2123 |
3.09e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1980 QKKIEDLQRQHQRELEKLREEKDRL--LAEETAATISA--------------IEAMKNAH-REEMER--ELEkSQRSQIS 2040
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVksLQTDSSNTDTAlttleealsekeriIERLKEQReREDRERleELE-SLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2041 SINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQR-ENQELNAHNQELNNRLAAEIT- 2118
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNPEINd 558
|
....*
gi 1907081936 2119 RLRTL 2123
Cdd:pfam10174 559 RIRLL 563
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1922-2210 |
3.32e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1922 GLRERIQELEAQMGVMREElgHKELEGDVAALQE----------KYQRDFESLKATceRGFAAMEETHQKKIEDLQRQHQ 1991
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEE--VDSLKSQLADYQQaldvqqtraiQYQQAVQALEKA--RALCGLPDLTPENAEDYLAAFR 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1992 RELEKLREEkdrLLAEETAATISaiEAMKNAHREEME------------------RELEKSQRSQiSSINSDIEALRRQY 2053
Cdd:COG3096 448 AKEQQATEE---VLELEQKLSVA--DAARRQFEKAYElvckiageversqawqtaRELLRRYRSQ-QALAQRLQQLRAQL 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2054 --LEELQSVQRELEVLSEQYSQ---KCLENA----HLAQALEAERQAL-----------RQCQRENQELNAHNQELNNRL 2113
Cdd:COG3096 522 aeLEQRLRQQQNAERLLEEFCQrigQQLDAAeeleELLAELEAQLEELeeqaaeaveqrSELRQQLEQLRARIKELAARA 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2114 AAEIT---RLRTLltgdggGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRdkkyasdkykdiyt 2190
Cdd:COG3096 602 PAWLAaqdALERL------REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIE-------------- 661
|
330 340
....*....|....*....|
gi 1907081936 2191 ELSIAKAKADCDISRLKEQL 2210
Cdd:COG3096 662 RLSQPGGAEDPRLLALAERL 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
809-979 |
3.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 809 QLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKK---LKRNYTL--- 882
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerlDASSDDLaal 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 883 --LLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQS 960
Cdd:COG4913 691 eeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170
....*....|....*....
gi 1907081936 961 LHDERDLIKHQFQELMERV 979
Cdd:COG4913 771 LEERIDALRARLNRAEEEL 789
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
756-898 |
3.60e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 756 EIQTLQTRLGNAAAELAIKEQALA---KLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELr 832
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL- 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081936 833 DLETQQALQRDRQkeVQRLQECIAELSQQLGTSEQAQRLMEKKlkrnytlllescEQEKQALLQNL 898
Cdd:PRK09039 126 DSEKQVSARALAQ--VELLNQQIAALRRQLAALEAALDASEKR------------DRESQAKIADL 177
|
|
| PH_DAPP1 |
cd10573 |
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ... |
69-145 |
3.64e-03 |
|
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269977 [Multi-domain] Cd Length: 96 Bit Score: 38.84 E-value: 3.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081936 69 WQRRFFILYEHgLLRYALDEMPTTlPQGTINMNQCTDVvDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEML 145
Cdd:cd10573 19 WKTRWFVLRRN-ELKYFKTRGDTK-PIRVLDLRECSSV-QRDYSQGKVNCFCLVFPERTFYMYANTEEEADEWVKLL 92
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1915-2179 |
3.88e-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: 42.74 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1915 DEAESMSGLRERIQELEAQMGVMREELG-----HKELEGDVAALQ------EKYQRDFESLKATcERGFAAME-ETHQKK 1982
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLDrlediLNELERQLKSLErqaekaERYKELKAELREL-ELALLVLRlEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1983 IEDLQRQhQRELEKLREEKDRLLAEETAAtisaIEAMKNAHREeMERELEKSQRS--QISSINSDIEALRRQYLEELQSV 2060
Cdd:TIGR02168 241 LEELQEE-LKEAEEELEELTAELQELEEK----LEELRLEVSE-LEEEIEELQKElyALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2061 QRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRtlltgdgggestglpltqg 2140
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE------------------- 375
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907081936 2141 kdayELEVLLRVKESEIQYLKQEISSLKDELQTALRDKK 2179
Cdd:TIGR02168 376 ----ELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1918-2094 |
3.98e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.32 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1918 ESMSGLRERIQELEAQMGVMREELgHKELEGDVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKL 1997
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQEL-VDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1998 ReekdrllaEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLE 2077
Cdd:pfam01442 83 R--------KRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154
|
170
....*....|....*...
gi 1907081936 2078 NA-HLAQALEAERQALRQ 2094
Cdd:pfam01442 155 RLqELREKLEPQAEDLRE 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1727-2114 |
4.21e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1727 EAKGASGQKRAQAVGALKEEYEELLHKQKSEYQKVITLIEKEN------TELKAkVSQMDHQQRCLQEAENKHSESMFAL 1800
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqmlAEEKA-ISARYAEERDRAEAEAREKETRALS 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1801 QGRYEEEIRCMVEQLSHTENTLQAERSRVLSQLDASVKD-------RQAMEQhHVQQMKM----LEDrfqlkvrELQAVH 1869
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhelersKRALEQ-QVEEMKTqleeLED-------ELQATE 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1870 QEELR------ALQEHYIWSLRgalslyqpshpdsslapgpsepravpaAKDEA--ESMSGLRERIQELEAQMGVMREEl 1941
Cdd:pfam01576 713 DAKLRlevnmqALKAQFERDLQ---------------------------ARDEQgeEKRRQLVKQVRELEAELEDERKQ- 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1942 ghkelEGDVAALQEKYQRDFESLKATCERGFAAMEET--HQKKIEDLQRQHQRELEKLREEKDRLLA--EETAATISAIE 2017
Cdd:pfam01576 765 -----RAQAVAAKKKLELDLKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRDEILAqsKESEKKLKNLE 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2018 A-----------------MKNAHREEMERELEK--SQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLEN 2078
Cdd:pfam01576 840 AellqlqedlaaserarrQAQQERDELADEIASgaSGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQV 919
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907081936 2079 AHLAQALEAERQALRQCQRENQELNAHNQELNNRLA 2114
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ 955
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1633-2211 |
4.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1633 IQDELAQQLREKASILEEISAALPVLPPT-EPLGGCQRLLRmsqhlSYESCLEGLgqySSLLVQDAIIQAQVCYAACRIR 1711
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELrEELEKLEKEVK-----ELEELKEEI---EELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1712 lEYEKELRFYKKACQEAKgaSGQKRAQAVGALKEEYEElLHKQKSEYQKVITLIEKENTELKAKVSQMdhqQRCLQEAEN 1791
Cdd:PRK03918 263 -ELEERIEELKKEIEELE--EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI---EERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1792 KHSEsMFALQGRyEEEIRCMVEQLSHTENTLQAERsRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQE 1871
Cdd:PRK03918 336 KEER-LEELKKK-LKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1872 ELRALqEHYIWSLRGALSLYQPSHPDSSL--APGPSEPRAVPAAKDEAEsMSGLRERIQELEAQMGVMREELghKELEGD 1949
Cdd:PRK03918 413 RIGEL-KKEIKELKKAIEELKKAKGKCPVcgRELTEEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKEL--RELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1950 VaalqeKYQRDFESLKATCERGFAAMEETHQKKIEDLQRQhQRELEKLREEKDRLLAE--ETAATISAIEAMKNaHREEM 2027
Cdd:PRK03918 489 L-----KKESELIKLKELAEQLKELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEikSLKKELEKLEELKK-KLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2028 ERELEKSQRsQISSINSDIEALRRQYLEELQSVQRELEVLSEQYsqkcLENAHLAQALEAERQALRQCQRENQELNAHNQ 2107
Cdd:PRK03918 562 EKKLDELEE-ELAELLKELEELGFESVEELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2108 ELNNRLAAEITRLRTLLTgdgggestglpLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTA------LRDKKYA 2181
Cdd:PRK03918 637 ETEKRLEELRKELEELEK-----------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIkktlekLKEELEE 705
|
570 580 590
....*....|....*....|....*....|
gi 1907081936 2182 SDKYKDIYTELSIAKAkadcDISRLKEQLK 2211
Cdd:PRK03918 706 REKAKKELEKLEKALE----RVEELREKVK 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
769-1046 |
5.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 769 AELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMlsgQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV 848
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM---ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 849 QRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLS 928
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 929 ETCKGSEQVHKLEEELEAREASIRQlaqhvqslHDERDLIKhqfQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHH 1008
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKK--------AEEENKIK---AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907081936 1009 RVSVQLQSVRTLLreKEEELKHIKETHERVLEKKDQDL 1046
Cdd:PTZ00121 1768 KKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
655-929 |
5.88e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVA--TSPSGAWQRlhrvnqdlQSELEAQCRRQELI 732
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQT--------ARELLRRYRSQQAL 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 733 TQQIQTLKHSYGEA-KDAIRHHEAEiqtlqtrlgnaaaelaikeqalaKLKGELKMEQGKVREQLEEWQHSKAMLSGQLR 811
Cdd:COG3096 511 AQRLQQLRAQLAELeQRLRQQQNAE-----------------------RLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 812 ASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTS--------EQAQRLMEKklKRNYTLL 883
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladsqevtAAMQQLLER--EREATVE 645
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907081936 884 LESCEQEKQALLQNLKEVEDKASAYEDQLqghVQQVEALQKEKLSE 929
Cdd:COG3096 646 RDELAARKQALESQIERLSQPGGAEDPRL---LALAERLGGVLLSE 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
655-820 |
5.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGY---VLQTEVAtspsgAWQ-RLHRVNQD------LQSELEA 724
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIA-----ELEaELERLDASsddlaaLEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 725 QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKA 804
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
170
....*....|....*.
gi 1907081936 805 MLSGQLRASEQKLRST 820
Cdd:COG4913 777 ALRARLNRAEEELERA 792
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1926-2070 |
7.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1926 RIQELEAQMGVMREELghKELEGDVAALQ---EKYQRDFESLKATCERgFAAMEETHQKKIEDLQRQH-----QRELEKL 1997
Cdd:COG1579 18 ELDRLEHRLKELPAEL--AELEDELAALEarlEAAKTELEDLEKEIKR-LELEIEEVEARIKKYEEQLgnvrnNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081936 1998 REEKDRLLAEETAATISAIEAMKNahREEMERELEKSQrSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2070
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMER--IEELEEELAELE-AELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
746-927 |
7.63e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 746 AKDAIRHHEAEIQTLQTRlGNAAAELAIKEQALAKLKGELKmeqgkVREQLEEwqhskamlsgQLRASEQKLRSTEARLL 825
Cdd:pfam09731 292 AHREIDQLSKKLAELKKR-EEKHIERALEKQKEELDKLAEE-----LSARLEE----------VRAADEAQLRLEFERER 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 826 EKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLgtseqaQRLMEKKLKrnytlllESCEQEKQALLQNLKEVEDKA 905
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIEL------QREFLQDIK-------EKVEEERAGRLLKLNELLANL 422
|
170 180
....*....|....*....|...
gi 1907081936 906 SAYEDQLQGHVQQV-EALQKEKL 927
Cdd:pfam09731 423 KGLEKATSSHSEVEdENRKAQQL 445
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
655-830 |
8.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 655 LEKELEQSQKEASDLLEQNRLLQ---DQLRVALGR------EQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEaq 725
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEaeiEERREELGEraralyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADAD-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 726 crrqelITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAM 805
Cdd:COG3883 134 ------LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
170 180
....*....|....*....|....*
gi 1907081936 806 LSGQLRASEQKLRSTEARLLEKTQE 830
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2012-2125 |
8.93e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 2012 TISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQA 2091
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110
....*....|....*....|....*....|....
gi 1907081936 2092 LRQCQRENQELNAHNQELNNRLAAEITRLRTLLT 2125
Cdd:pfam09787 123 LRYLEEELRRSKATLQSRIKDREAEIEKLRNQLT 156
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1913-2058 |
9.00e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081936 1913 AKDEAESMSGLRERIQELEAQMGVMREELG----HKELEGDVAALQ-EKYQRDFESLKatcergfaameETHQKKIEDLQ 1987
Cdd:pfam15397 76 EEKEESKLNKLEQQLEQLNAKIQKTQEELNflstYKDKEYPVKAVQiANLVRQLQQLK-----------DSQQDELDELE 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081936 1988 RQHQRELEKL----REEKDRLL---AEETAATISAIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQyLEELQ 2058
Cdd:pfam15397 145 EMRRMVLESLsrkiQKKKEKILsslAEKTLSPYQESLLQKTRDNQVMLKEIEQ-FREFIDELEEEIPKLKAE-VQQLQ 220
|
|
| |
