|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1477-1767 |
1.79e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 390.50 E-value: 1.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1477 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1554
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1555 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1627
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1628 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1703
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 1704 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1767
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-260 |
9.75e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 9.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613727 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.53e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613727 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-223 |
1.45e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1240-1870 |
1.27e-09 |
|
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: 63.60 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1240 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1315
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1316 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1385
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1386 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1465
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1466 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1543
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1544 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1620
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1621 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1690
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1691 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1764
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1765 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1838
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 1034613727 1839 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1870
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1483-1838 |
3.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1483 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1551
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1552 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1621
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1622 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1700
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1701 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1779
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613727 1780 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1838
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1363-1848 |
3.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1363 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1442
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1443 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1522
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1523 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1602
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1603 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1682
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1683 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1761
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1762 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1841
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 1034613727 1842 QKLEVEH 1848
Cdd:COG4717 470 ELAELLQ 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1357-1769 |
1.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1429
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1430 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1507
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1508 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1587
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1588 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1666
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1667 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1744
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 1034613727 1745 MLVNELNHSKEKECQYEKEKAEREV 1769
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
92-229 |
1.31e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
....*..
gi 1034613727 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1362-1569 |
2.03e-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: 48.99 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1362 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1433
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1434 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1512
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613727 1513 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1569
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
114-220 |
1.65e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.54 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192 66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034613727 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.94e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.94e-04
10 20
....*....|....*....|....*....
gi 1034613727 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
728-946 |
2.05e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.58 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108 1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108 1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
544-1119 |
6.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 544 KVSSQKQPAEKATSDDKDSVSNIATEIKEGPISGTVSSQK----QPAEKATSDEKDSVSNIATEIKKGQQSGTVSPQKQS 619
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 620 AWKvifKKKVSLLNiatrimggGKSGTVSSQKQPASKATSDKTDSALNIATEIKDGLQCGTVSSQKQPALKATTDEEDSV 699
Cdd:PTZ00121 1311 AEE---AKKADEAK--------KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 700 SNIATEIKDGEKSGTVSSQKQPALKATTDEedsVSNIATEIKDGEKSGTVSSQKQPA--LKATTDEK---DSVSNIATEI 774
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAkkaDEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 775 KDGEKSGTVSSQKPPALTATSD-EEGSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSFSNITRGK--KDGEISRKV 851
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 852 SSQKPPTLKGTSDE--EDSVLGIARENKDGEKSRTVSSEKPPGLK----ASSAEKDSVLNIARGKKDGEKTKRVSSRKKP 925
Cdd:PTZ00121 1537 DEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 926 SLEATSDEKDSFSNItrEKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSRTVSSEKPpglKATSDEKDSV 1005
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---KAEEDEKKAA 1691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1006 LniARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSVLYIAREKKDGEK 1085
Cdd:PTZ00121 1692 E--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
570 580 590
....*....|....*....|....*....|....
gi 1034613727 1086 SRTVSSPKQPALKAICDKEDSVPNMATEKKDEQI 1119
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1357-1594 |
2.26e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1435
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1436 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1507
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1508 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1587
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 1034613727 1588 KRDQELA 1594
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1346-1575 |
3.60e-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: 42.36 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1346 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1425
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1426 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1505
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1506 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1575
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1477-1767 |
1.79e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 390.50 E-value: 1.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1477 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1554
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1555 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1627
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1628 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1703
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 1704 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1767
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-260 |
9.75e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 9.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613727 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
28-266 |
2.24e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.73 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 28 IKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:COG0666 17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 108 LRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:COG0666 97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613727 188 ANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDLPINSNP 266
Cdd:COG0666 177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-233 |
6.30e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 147.79 E-value: 6.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034613727 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIA 233
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-201 |
3.51e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.37 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 1034613727 196 LGRSAL 201
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-252 |
2.18e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 111.20 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 45 LEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP 124
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 125 NITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHA 204
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034613727 205 VTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEY 252
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.53e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613727 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-223 |
1.45e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
135-227 |
3.20e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 135 LHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKkANVNAIDYlGRSALIHAVTLGEKDIVI 214
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613727 215 LLLQHNIDVLSRD 227
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
44-249 |
2.00e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.24 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGAN 123
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 124 PNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKvKMVEfLLKKKANVNAIDYLGRSALIH 203
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIE-LLINNASINDQDIDGSTPLHH 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034613727 204 AVTLG-EKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNR--VIFDLI 249
Cdd:PHA02874 261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
102-194 |
7.68e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 102 LIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGtNIEECSKcEYQPLLFAVSRRKVKMVE 181
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613727 182 FLLKKKANVNAID 194
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
51-205 |
2.33e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.00 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 51 LLLTY-YDANKRDR-KERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITD 128
Cdd:PHA02878 152 LLLSYgADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 129 FFGRTALHYAV-YNEDTSMIEKLLSHGTNIEECSKC-EYQPLLFAV-SRRKVKMvefLLKKKANVNAIDYLGRSALIHAV 205
Cdd:PHA02878 232 KCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIkSERKLKL---LLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-280 |
2.31e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 32 HLKRIHRAVLHGNL--------EKLKYLLLTYYDANKRDRKERTALHLacatgqpemvhlLVSRRCElnlcdredrtPLI 103
Cdd:PHA03095 6 SVDIIMEAALYDYLlnasnvtvEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSE----------KVK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 104 KAVQLrqeacatlLLQNGANPNITDFFGRTALHYAVYNEDT-SMIEKLLSHGTNIEECSKCEYQPL--LFAVSRRKVKMV 180
Cdd:PHA03095 64 DIVRL--------LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 181 EFLLKKKANVNAIDYLGRSALihAVTLGEKDIvilllqhNIDVLsRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEdl 260
Cdd:PHA03095 136 RLLLRKGADVNALDLYGMTPL--AVLLKSRNA-------NVELL-RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAR-- 203
|
250 260
....*....|....*....|
gi 1034613727 261 pINSNPVSSQKQPALKATSG 280
Cdd:PHA03095 204 -IVRELIRAGCDPAATDMLG 222
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
100-223 |
4.79e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.55 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 100 TPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHY-----AVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSR 174
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 175 RK--VKMVEFLLKKKANVNAIDYLGRSaLIHAVTLG---EKDIVILLLQHNIDV 223
Cdd:PHA03100 117 KSnsYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESnkiDLKILKLLIDKGVDI 169
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-222 |
7.90e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 72.72 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 39 AVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSR-----------RCELN-------------LC 94
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaipdvkypdiESELHdaveegdvkaveeLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 95 D----------REDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECsk 162
Cdd:PHA02875 89 DlgkfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKacLDIEDC-- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 163 CEYQPLLFAVSRRKVKMVEFLLKKKANvnaIDYLGR----SALIHAVTLGEKDIVILLLQHNID 222
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKngcvAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
32-252 |
4.02e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRT----------- 100
Cdd:PHA02876 145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdskni 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 101 ------------------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS-MIEKLLSHGTNIEECS 161
Cdd:PHA02876 225 dtikaiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 162 KCEYQPL-LFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGE-KDIVILLLQHNIDVLSRDAFRKIAGDYAIE 239
Cdd:PHA02876 305 IKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAV 384
|
250
....*....|...
gi 1034613727 240 AKNRVIFDLIYEY 252
Cdd:PHA02876 385 RNNVVIINTLLDY 397
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
36-223 |
1.03e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.01 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKL-KYLLLTYYDANKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 112
Cdd:PHA02876 277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 113 CATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKM-VEFLLKKKANVN 191
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
|
170 180 190
....*....|....*....|....*....|...
gi 1034613727 192 AIDYLGRSALIHAVTLGEK-DIVILLLQHNIDV 223
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADV 469
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
36-193 |
1.03e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKE-RTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACA 114
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 115 TLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLL-FAVSRRKVKMVEFLLKKKANVNAI 193
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-194 |
2.00e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 30 PYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPLIKAVq 107
Cdd:PHA03100 71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 108 lrqEACAT------LLLQNGANPN----------------ITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEY 165
Cdd:PHA03100 150 ---ESNKIdlkilkLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180
....*....|....*....|....*....
gi 1034613727 166 QPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1240-1870 |
1.27e-09 |
|
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: 63.60 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1240 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1315
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1316 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1385
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1386 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1465
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1466 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1543
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1544 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1620
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1621 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1690
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1691 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1764
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1765 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1838
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 1034613727 1839 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1870
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
99-151 |
1.31e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 1.31e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 99 RTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLL 151
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
32-85 |
3.18e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 3.18e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLV 85
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
36-255 |
6.44e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 116 LLLQNGANPNITDFFGRTALHYAV-YNEdtSMIEKLLSHGTnIEECSKCEYQPLLFAVSRR-KVKMVEFLLKKKANVNAI 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIELLINNAS-INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613727 194 DYLGRSALIHAVTLGEKDIVILLLQHNIdVLSRDAFRKIAGDY--AIEAK-NRVIFDLIYEYERK 255
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVIKDIIANA-VLIKEADKLKDSDFleHIEIKdNKEFSDFIKECNEE 348
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
44-194 |
8.45e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.04 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 120
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613727 121 ---GANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03095 244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
67-226 |
2.72e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.44 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 67 TALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP---------------------- 124
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 125 -NITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECSKCeyQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSAL 201
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGadVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
170 180
....*....|....*....|....*
gi 1034613727 202 IHAVTLGEKDIVILLLQHNIDVLSR 226
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNK 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1483-1838 |
3.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1483 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1551
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1552 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1621
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1622 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1700
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1701 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1779
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613727 1780 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1838
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
131-184 |
4.89e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 4.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLL 184
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1360-1871 |
5.82e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.06 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1360 RVKIRKLKNKASVLQKRISEKE---EIKSQLKHEILE-LEKELCSLRFAIQQEKkkrrnveEVHQKVREKLRITEEQYRI 1435
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTlctPCMPDTYHERKQvLEKELKHLREALQQTQ-------QSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1436 EAdvtkpikpALKSAEVELKTGGNNSNQVSETDEKED--------LLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDF 1507
Cdd:TIGR00618 259 QQ--------LLKQLRARIEELRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1508 EIVKRKHEDLQKALKRNGETLAKTIacysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlNAARCDHDQSHSS 1587
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEI-----HIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-----KTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1588 KRDQELAFQGTVDKCRHLQENLNSHVLIL--SLQLSKAESKSRVLKTELHYTGEALKEKALVfEHVQS--ELKQKQSQMK 1663
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSlkEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1664 DIEKMYKSGYNTMEKCIEK-QERFCQLKKQNMLLQQQLDDARNKADNQEK--AILNIQARCDARVQNLQAEC---RKHRL 1737
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLElQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqRGEQTYAQLETSEEDVYHQLtseRKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1738 LLEEDnkmlVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGS-ATKALLDASSRHCTYLENGMQDSRKKLDQm 1816
Cdd:TIGR00618 560 SLKEQ----MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeAEDMLACEQHALLRKLQPEQDLQDVRLHL- 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613727 1817 rSQFQEIQDQLTATIrcTKEMEGDTQKLEVEHVMMRKIIKKQDDQI-ERLEKILQH 1871
Cdd:TIGR00618 635 -QQCSQELALKLTAL--HALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQS 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1360-1724 |
7.21e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1360 RVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRIEAD 1438
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1439 VTKPIKpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ-NLEKKYLKDFEIVKRKHEDL 1517
Cdd:TIGR02168 756 LTELEA---EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1518 QKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQG 1597
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1598 TVDKCRHLQENLNSHVlilsLQLSKAESKSRVLKTEL--HY--TGEALKEKALVFEHVQSELKQKQSQMK-DIEKMYKSG 1672
Cdd:TIGR02168 913 LRRELEELREKLAQLE----LRLEGLEVRIDNLQERLseEYslTLEEAEALENKIEDDEEEARRRLKRLEnKIKELGPVN 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034613727 1673 YNTMEKCIEKQERFCQLKKQnmllQQQLDDARNKAdnqEKAILNIQARCDAR 1724
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQ----KEDLTEAKETL---EEAIEEIDREARER 1033
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
36-259 |
1.83e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.80 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTY-YDANKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQE 111
Cdd:PHA03095 87 LHLYLYNATTLDVIKLLIKAgADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 112 ACAT----LLLQNGANPNITDFFGRTALHY---------AVYNEDT----------------------------SMIEKL 150
Cdd:PHA03095 164 NANVellrLLIDAGADVYAVDDRFRSLLHHhlqsfkpraRIVRELIragcdpaatdmlgntplhsmatgssckrSLVLPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 151 LSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL--QHNIDVLSR-- 226
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALakNPSAETVAAtl 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034613727 227 DAFRKIAGDYAIEAKNRVI--------FDLIYEYERKRYED 259
Cdd:PHA03095 324 NTASVAGGDIPSDATRLCVakvvlrgaFSLLPEPIRAYHAD 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1344-1665 |
2.09e-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: 56.22 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1344 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcslrfaiqQEKKKRRN--VEEVHQK 1421
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--------EELQKELYalANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1422 VREKLRITEEQYRIEADvtkpikpaLKSAEVELKTGGnnsnqvSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEK 1501
Cdd:TIGR02168 301 EQQKQILRERLANLERQ--------LEELEAQLEELE------SKLDELAEELAE---LEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1502 KylKDFEIVKRKHEDLQKALkrngETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH 1581
Cdd:TIGR02168 364 E--AELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1582 DQSHSSKRDQELAfqgtvdKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQS------EL 1655
Cdd:TIGR02168 438 LQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkAL 511
|
330
....*....|
gi 1034613727 1656 KQKQSQMKDI 1665
Cdd:TIGR02168 512 LKNQSGLSGI 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1363-1848 |
3.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1363 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1442
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1443 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1522
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1523 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1602
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1603 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1682
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1683 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1761
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1762 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1841
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 1034613727 1842 QKLEVEH 1848
Cdd:COG4717 470 ELAELLQ 476
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
164-217 |
1.48e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 164 EYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
100-226 |
2.11e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 100 TPLIKAVQLRQEACATLLLQNGANPN-------------------------------ITDFF---GRTALHYAVYNEDTS 145
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDvkypdieselhdaveegdvkaveelldlgkfADDVFykdGMTPLHLATILKKLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 146 MIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQH--NIDV 223
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDY 196
|
...
gi 1034613727 224 LSR 226
Cdd:PHA02875 197 FGK 199
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
43-192 |
2.63e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 43 GNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--N 120
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaS 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034613727 121 GANPNItdffGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNA 192
Cdd:PLN03192 616 ISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-105 |
3.81e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 3.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034613727 57 DANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 105
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
65-118 |
5.10e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 5.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 65 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
72-223 |
6.30e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.41 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 72 ACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSmIEKLL 151
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034613727 152 SHGTNIEEcSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PLN03192 611 YHFASISD-PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
36-225 |
1.22e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.88 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrrcELNLCDREDRTPLIK-AVQLRQEACA 114
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYTLVAIKdAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 115 TLLLQNG--ANPNITDFFGRTALHYAVYneDTSMIEKLLSHGTNIEECSK-CEYQPLLFAVSRRKVKMVEFLLKKKANVN 191
Cdd:PHA02878 118 KIILTNRykNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034613727 192 AIDYLGRSALIHAVTLGEKDIVILLLQH--NIDVLS 225
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENgaSTDARD 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1357-1769 |
1.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1429
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1430 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1507
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1508 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1587
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1588 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1666
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1667 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1744
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 1034613727 1745 MLVNELNHSKEKECQYEKEKAEREV 1769
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
92-229 |
1.31e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
....*..
gi 1034613727 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1378-1881 |
1.61e-05 |
|
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: 50.17 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1378 SEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTG 1457
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1458 GNNSNQVSETDEKedLLHENRLMQDEIARL--RLEKDTIKNQNLEKkylkdfeiVKRKHE----DLQKALKRNGET---L 1528
Cdd:pfam01576 137 EEDILLLEDQNSK--LSKERKLLEERISEFtsNLAEEEEKAKSLSK--------LKNKHEamisDLEERLKKEEKGrqeL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1529 AKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQElafqgtvDKCRHLQEN 1608
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-------AQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1609 LNSHvlilSLQLSKAESKSRVLKTELhytgEALK---EKALVFEHVQSELKQKQSQMkdiekmyksgYNTMEKCIEKQER 1685
Cdd:pfam01576 280 LESE----RAARNKAEKQRRDLGEEL----EALKtelEDTLDTTAAQQELRSKREQE----------VTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1686 FCQLKKQNML---------LQQQLDDARNKADNQEKAilniqarcdarvqnlqaecrkhRLLLEEDNKMLVNELNHSKEK 1756
Cdd:pfam01576 342 SHEAQLQEMRqkhtqaleeLTEQLEQAKRNKANLEKA----------------------KQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1757 ECQYEKEKAEREVAVRQLQQK-------RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTA 1829
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARlseserqRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034613727 1830 TIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKilQHSSLMLQVFES 1881
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER--QLSTLQAQLSDM 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1346-1667 |
1.65e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1346 KRLIKLKDNHCEQLRVKI---RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKK----KRRNVEEV 1418
Cdd:TIGR02169 198 QQLERLRREREKAERYQAllkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1419 HQKVREKlrITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQn 1498
Cdd:TIGR02169 278 NKKIKDL--GEEEQLRVKEKI----------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1499 lekkyLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEK---QRESRQRLETEMQSYHCRLN 1575
Cdd:TIGR02169 345 -----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1576 AARCDHDQSHSSKRDQELAFQGTVD----KCRHLQENLNShvliLSLQLSKAESKSRVLKTELhytgealkekalvfEHV 1651
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQ----LAADLSKYEQELYDLKEEY--------------DRV 481
|
330
....*....|....*.
gi 1034613727 1652 QSELKQKQSQMKDIEK 1667
Cdd:TIGR02169 482 EKELSKLQRELAEAEA 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1362-1569 |
2.03e-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: 48.99 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1362 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1433
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1434 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1512
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613727 1513 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1569
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1357-1784 |
3.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1436
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1437 ADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhenrlmQDEIARLrlekdtiknqnleKKYLKDFEIVKRKHED 1516
Cdd:PRK03918 314 KRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL------EKRLEEL-------------EERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1517 LQKALKR-NGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlnaarcdhdqshsskrdqelaf 1595
Cdd:PRK03918 374 LERLKKRlTGLTPEKLEK----ELEELEKAKEEIEEEISKITARIGELKKEIKE-------------------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1596 qgtvdkcrhLQENLNshvlilslQLSKAESKSRVLKTEL--HYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSgy 1673
Cdd:PRK03918 424 ---------LKKAIE--------ELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1674 ntMEKCIEKQERFCQLKKqnmlLQQQLDDARNKAD--NQEKailniqarcdarvqnLQAECRKHRLLLEEDNKML--VNE 1749
Cdd:PRK03918 485 --LEKVLKKESELIKLKE----LAEQLKELEEKLKkyNLEE---------------LEKKAEEYEKLKEKLIKLKgeIKS 543
|
410 420 430
....*....|....*....|....*....|....*
gi 1034613727 1750 LNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK 1784
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1348-1871 |
4.11e-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: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1348 LIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVRE-KL 1426
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQlKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1427 RITEEQYRIEA------DVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQDEIARLRLEKDtiKNQNLE 1500
Cdd:TIGR04523 233 NIEKKQQEINEktteisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNNQ--KEQDWN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1501 KKYLKDFEIVKRKHEDLQKALKRNGET---LAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNaa 1577
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1578 rcdhdQSHSSKRDQELAFQGTVDKCRHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQ 1657
Cdd:TIGR04523 388 -----NLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1658 KQSQMKDIEKMYKSGYNTMEKCIEKQerfcqlkkqnmllQQQLDDarnkaDNQEKAILNIQARcdarvqnlqaecrkhrl 1737
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK-------------QKELKS-----KEKELKKLNEEKK----------------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1738 LLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQ---KRDDVLNKGSATKAL------LDASSRHCTYLENGMQD 1808
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnKDDFELKKENLEKEIdeknkeIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 1809 SRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQH 1871
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1249-1777 |
6.10e-05 |
|
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: 48.18 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1249 KMKDVqtSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDI-------IQSSQTVSEDgdsLCCNCKNVILL 1321
Cdd:pfam05483 255 KMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrsMSTQKALEED---LQIATKTICQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1322 IDQHEMKCKD-----CVHLL---KIKNTFCLWKRLIKLK----DNHCEQLRVKIRKLKNKASVLQkrisEKEEIKSQLKH 1389
Cdd:pfam05483 330 TEEKEAQMEElnkakAAHSFvvtEFEATTCSLEELLRTEqqrlEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1390 EILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYR------IEADVTKPIKPALKSAEVELKTGGNNS-- 1461
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdleIQLTAIKTSEEHYLKEVEDLKTELEKEkl 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1462 NQVSETDEKEDLLHENRLMQDEIARLRLEkdtiknqnlekkylkdfeiVKRKHEDLQKALKRNGETLAktiacysgQLAA 1541
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLE-------------------LKKHQEDIINCKKQEERMLK--------QIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1542 LTDENTTLRSKLEKQRESRQRLETEMQsyhCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLnshvlilslqls 1621
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVK---CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI------------ 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1622 kaESKSRVLKtELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLlqQQLD 1701
Cdd:pfam05483 604 --ENKNKNIE-ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL--EEVE 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613727 1702 DARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQK 1777
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-154 |
7.25e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGANPNITDFFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110
....*....|....*....|....*....|.
gi 1034613727 133 TALHYAVYNED---------TSMIEKLLSHG 154
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLL 240
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
98-229 |
7.96e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 98 DRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKV 177
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034613727 178 KMVEFLLKKKANVNAIDYLGRSALIHAVTLGEK-DIVILLLQH--NIDVLSRDAF 229
Cdd:PHA02875 82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKlDIMKLLIARgaDPDIPNTDKF 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1357-1569 |
9.05e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1436
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1437 ADVTKpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHED 1516
Cdd:COG1196 364 EEALL----EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 1517 LQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1569
Cdd:COG1196 440 EEEALEEAAEEEAELEE----EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
83-138 |
1.47e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613727 83 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYA 138
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1344-1625 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1344 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVR 1423
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1424 EKLR-ITEEQYRIEADVTkpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKK 1502
Cdd:COG1196 309 ERRReLEERLEELEEELA-----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1503 YLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHD 1582
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034613727 1583 QSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1625
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
114-220 |
1.65e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.54 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192 66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034613727 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.94e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.94e-04
10 20
....*....|....*....|....*....
gi 1034613727 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
728-946 |
2.05e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.58 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108 1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108 1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
51-107 |
2.24e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613727 51 LLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
117-171 |
2.43e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 2.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613727 117 LLQNG-ANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFA 171
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1386-1716 |
2.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1386 QLKHEILELEKELCSLRFAIQQEKKKRRNvEEVHQKVREKLRITEEQYRIEAdvtkpikpALKSAEVELKTggnnsnqvs 1465
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE-AELEELEAELEELEAELAELEA--------ELEELRLELEE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1466 ETDEKEDLLHENRLMQDEIArlRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDE 1545
Cdd:COG1196 279 LELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1546 NTTLRSKLEKQRESRQRLETEMQsyhcrlnaarcDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1625
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1626 KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKsgyntmekciEKQERFCQLKKQNMLLQQQLDDARN 1705
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA----------ELLEEAALLEAALAELLEELAEAAA 491
|
330
....*....|.
gi 1034613727 1706 KADNQEKAILN 1716
Cdd:COG1196 492 RLLLLLEAEAD 502
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
139-222 |
2.72e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 139 VYNEDTSMIEKLLSHGTNIEECSKCE-YQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
....*
gi 1034613727 218 QHNID 222
Cdd:PHA02874 89 DNGVD 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1350-1741 |
3.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1350 KLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKvREKLRIT 1429
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-ELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1430 EEQYRIEADVtKPIKPALKSAEVELKtggnnsnQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYlKDFEI 1509
Cdd:PRK03918 459 AELKRIEKEL-KEIEEKERKLRKELR-------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-EEYEK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1510 VKRKHEDLQKALKRNGETLAKtiacysgqLAALTDENTTLRSKLEKQRESRQRLETEMQSY--------HCRLNAARCDH 1581
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEK--------LEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1582 DQSHSSKrDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES-KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQS 1660
Cdd:PRK03918 602 NEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEElRKELEELEKKYSEEEYEELREEYLELSRELAGLRA 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1661 QMKDIEKMYKsgynTMEKCIEKQERfcQLKKqnmllqqqLDDARNKADNQEKAIlniqarcdARVQNLQAECRKHRLLLE 1740
Cdd:PRK03918 681 ELEELEKRRE----EIKKTLEKLKE--ELEE--------REKAKKELEKLEKAL--------ERVEELREKVKKYKALLK 738
|
.
gi 1034613727 1741 E 1741
Cdd:PRK03918 739 E 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1352-1838 |
4.07e-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: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1352 KDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITE 1430
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1431 EqyrieadvtkpikpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiV 1510
Cdd:pfam05483 332 E----------------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------L 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1511 KRKHEDLQK--ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRL-------ETEMQSYHCRLNAARCdh 1581
Cdd:pfam05483 387 QKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKT-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1582 DQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYtgealkekalvfEHVQSELKQKQSQ 1661
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------EDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1662 MKDIEkmyksgyNTMEKCIEKQERFCQLKKQnmlLQQQLDDARNKADNQEKAILNIQARCdarvqnlqaecrkhrLLLEE 1741
Cdd:pfam05483 533 LKQIE-------NLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEV---------------LKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1742 DNKMLVNELNHSKekecqyeKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1821
Cdd:pfam05483 588 QMKILENKCNNLK-------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
490
....*....|....*...
gi 1034613727 1822 -EIQDQLTATIRCTKEME 1838
Cdd:pfam05483 661 kEIEDKKISEEKLLEEVE 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1357-1867 |
4.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEK----EEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQ 1432
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1433 YRIEADVTKpiKPALKSAEVELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIV 1510
Cdd:PTZ00121 1398 KKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1511 KRKHEDLQKA--LKRNGETLAKTiacysgqlaalTDEnttLRSKLEKQRESRQRLETEmqsyhcrlNAARCDHDQSHSSK 1588
Cdd:PTZ00121 1476 KKKAEEAKKAdeAKKKAEEAKKK-----------ADE---AKKAAEAKKKADEAKKAE--------EAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1589 RdqelafqgTVDKCRHLQENLNSHVLILSLQLSKAESKSRVlktELHYTGEALKEKAL--VFEHVQSELKQKQSQMKDIE 1666
Cdd:PTZ00121 1534 K--------KADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1667 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAilnIQARCDARVQNLQAECRKHRlllEEDNKML 1746
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA---EELKKAEEENKIKAAEEAKK---AEEDKKK 1676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1747 VNELNHSKEKECQYE---KEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSqfQEI 1823
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK--DEE 1754
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034613727 1824 QDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEK 1867
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
36-187 |
5.48e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 36 IHRAVLHGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 100
Cdd:cd22192 55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 101 --------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 162
Cdd:cd22192 131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210
|
170 180
....*....|....*....|....*
gi 1034613727 163 CEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd22192 211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
90-229 |
6.17e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 90 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNI--EECSKCE 164
Cdd:cd22192 7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 165 YQ---PLLFAVSRRKVKMVEFLLKKKANVN--------------AIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRD 227
Cdd:cd22192 87 YQgetALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
..
gi 1034613727 228 AF 229
Cdd:cd22192 167 SL 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
544-1119 |
6.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 544 KVSSQKQPAEKATSDDKDSVSNIATEIKEGPISGTVSSQK----QPAEKATSDEKDSVSNIATEIKKGQQSGTVSPQKQS 619
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 620 AWKvifKKKVSLLNiatrimggGKSGTVSSQKQPASKATSDKTDSALNIATEIKDGLQCGTVSSQKQPALKATTDEEDSV 699
Cdd:PTZ00121 1311 AEE---AKKADEAK--------KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 700 SNIATEIKDGEKSGTVSSQKQPALKATTDEedsVSNIATEIKDGEKSGTVSSQKQPA--LKATTDEK---DSVSNIATEI 774
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAkkaDEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 775 KDGEKSGTVSSQKPPALTATSD-EEGSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSFSNITRGK--KDGEISRKV 851
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 852 SSQKPPTLKGTSDE--EDSVLGIARENKDGEKSRTVSSEKPPGLK----ASSAEKDSVLNIARGKKDGEKTKRVSSRKKP 925
Cdd:PTZ00121 1537 DEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 926 SLEATSDEKDSFSNItrEKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSRTVSSEKPpglKATSDEKDSV 1005
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---KAEEDEKKAA 1691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1006 LniARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSVLYIAREKKDGEK 1085
Cdd:PTZ00121 1692 E--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
570 580 590
....*....|....*....|....*....|....
gi 1034613727 1086 SRTVSSPKQPALKAICDKEDSVPNMATEKKDEQI 1119
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1364-1879 |
8.77e-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: 44.44 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1364 RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQE--------KKKRRNVEEVHQKVREKLRITEEQYRI 1435
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaadaavAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1436 EADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLmQDEIARLRLEKDTIKN-------------QNLEKK 1502
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREardrqlavaeddlQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1503 YLKDFEIVKRKHEDLQKALKRNGETLAKTI--ACYSG----QLAALTDENTTLRSKLEKQRESRQRLETEmqsyhcrLNA 1576
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKSRLGELKLRLnqATATPelllQLENFDERIERAREEQEAANAEVERLQSE-------LRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1577 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN--SHVLILSLQLSKA---ESKSRVLKTELhytgeaLKEKALVFEHV 1651
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqAGTLLHFLRKEAPdweQSIGKVISPEL------LHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1652 QSELKQKQSQMK---DIEKMYKSGYNTMEKciekqerfcQLKKQNMLLQQQLDDARNKADNQEKAILNIqarcDARVQNL 1728
Cdd:pfam12128 571 DGSVGGELNLYGvklDLKRIDVPEWAASEE---------ELRERLDKAEEALQSAREKQAAAEEQLVQA----NGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1729 QAECRKHRLLLE---EDNKMLVNELNHSKEK-ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKA-----LLDASSRHC 1799
Cdd:pfam12128 638 SREETFARTALKnarLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEKQ 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1800 TYLENGMQDSRKKLDQMRSQFQEIQDQLTATIR-CTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQV 1878
Cdd:pfam12128 718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
.
gi 1034613727 1879 F 1879
Cdd:pfam12128 798 F 798
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
168-254 |
8.95e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.47 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 168 LLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFD 247
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....*..
gi 1034613727 248 LIYEYER 254
Cdd:PLN03192 609 ILYHFAS 615
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-187 |
1.64e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 64 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGANP---NIT 127
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613727 128 DFFGRTALHYAVYNED---------TSMIEKLLSHGTNIEECSKCE-------YQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd21882 152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQLEeipnhqgLTPLKLAAVEGKIVMFQHILQRE 227
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-96 |
1.71e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 1.71e-03
10 20 30
....*....|....*....|....*....|..
gi 1034613727 66 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 96
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-93 |
2.24e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 2.24e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1357-1594 |
2.26e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1435
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1436 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1507
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1508 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1587
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 1034613727 1588 KRDQELA 1594
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1649-1867 |
2.59e-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: 42.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1649 EHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARnKADNQEKAILNiqarcdARVQNL 1728
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE------ARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1729 QAECRKHRLLLEEdnkmLVNELNHSKEKECQYEKEKAEREVA-----VRQLQQKrddvLNKGSATKALLDASSRHctyLE 1803
Cdd:TIGR02169 771 EEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSriearLREIEQK----LNRLTLEKEYLEKEIQE---LQ 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613727 1804 NGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKiikkqddQIERLEK 1867
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-------ERDELEA 896
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1345-1874 |
2.85e-03 |
|
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: 42.70 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1345 WKRLIKLKDNHCEQLRVKIRKLKN-------KASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEE 1417
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNelknkekELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1418 VHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ 1497
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK--FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1498 NLEKKYlkdfEIVKRKHEDLQKALK-RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNA 1576
Cdd:TIGR04523 182 KLNIQK----NIDKIKNKLLKLELLlSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1577 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN---SHVLILSLQ------------LSKAESKSRVLKTELHYTGEAL 1641
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1642 KEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQErfcQLKKQNMLLQQQLDDARNKADNQEKailnIQARC 1721
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEK----LNQQK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1722 DARVQNLQAEcrkhRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTY 1801
Cdd:TIGR04523 411 DEQIKKLQQE----KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034613727 1802 LENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSL 1874
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1346-1575 |
3.60e-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: 42.36 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1346 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1425
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1426 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1505
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1506 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1575
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
863-1087 |
3.65e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 863 SDEEDSVLGIARENKDGEKSRTVSSE---KPPGLKASSAEKDSVLNIaRGKKDGEKTKRVSSRKKPSLEATSDEKDSFSN 939
Cdd:PTZ00108 1143 EQEEVEEKEIAKEQRLKSKTKGKASKlrkPKLKKKEKKKKKSSADKS-KKASVVGNSKRVDSDEKRKLDDKPDNKKSNSS 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 940 IT------------REKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSRTVSSEKPPGLKATSDEK----D 1003
Cdd:PTZ00108 1222 GSdqeddeeqktkpKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESnggsK 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1004 SVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSVLYIAREKKDG 1083
Cdd:PTZ00108 1302 PSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDD 1381
|
....
gi 1034613727 1084 EKSR 1087
Cdd:PTZ00108 1382 EDDE 1385
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1589-1863 |
3.68e-03 |
|
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: 42.42 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1589 RDQELAFQgtVDKCRHLQEnlnshvlilsLQLSKAESKSRVlKTELhytgEALKEKALVFEHVQSELKQKQSQMKDIEKM 1668
Cdd:pfam17380 366 RQEEIAME--ISRMRELER----------LQMERQQKNERV-RQEL----EAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1669 YKSGYN-TMEKCIEKQER-FCQLKKQNMLLQQQLDDARNKADNQEKAILNiqarcdarvqnLQAECRKHRLLLEEDNKML 1746
Cdd:pfam17380 429 QEEARQrEVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLE-----------LEKEKRDRKRAEEQRRKIL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1747 VNELNHSKEKECQ-------YEKEKAEREVAVRQLQQKRDdvlnkgsatkalldassrhctylengMQDSRKKLDQMRSQ 1819
Cdd:pfam17380 498 EKELEERKQAMIEeerkrklLEKEMEERQKAIYEEERRRE--------------------------AEEERRKQQEMEER 551
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034613727 1820 fQEIQDQltatIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIE 1863
Cdd:pfam17380 552 -RRIQEQ----MRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
131-162 |
3.69e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.69e-03
10 20 30
....*....|....*....|....*....|...
gi 1034613727 131 GRTALHYAVYNE-DTSMIEKLLSHGTNIEECSK 162
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1357-1871 |
5.36e-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: 41.88 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRiSEKEEIKSQLKHEILELEKELCSLrfAIQQEKKKRRnveevhqkvREKLRITEEQYRIE 1436
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVL--EETQERINRA---------RKAAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1437 ------ADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARL----RLEKDTIKNQNLEKKYLKD 1506
Cdd:TIGR00618 304 qieqqaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhevaTSIREISCQQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1507 FEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH-DQSH 1585
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1586 SSKRDQELAFQGTVDKCRHLQENlNSHVLILSLQLSKAESKSRVLKTELHYTGEAlkEKALVFEHVQSELKQKQSQMKDI 1665
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPAR--QDIDNPGPLTRRMQRGEQTYAQL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1666 EKmykSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDdARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKM 1745
Cdd:TIGR00618 541 ET---SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1746 LVNELNHSKEK------ECQYEKEKAEREVAVRQLQQK--RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMR 1817
Cdd:TIGR00618 617 LLRKLQPEQDLqdvrlhLQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613727 1818 SQFQEIQDQLtatiRC--TKEMEGDTQKLEVEHVMMRKI--IKKQDDQIERLEKILQH 1871
Cdd:TIGR00618 697 EMLAQCQTLL----REleTHIEEYDREFNEIENASSSLGsdLAAREDALNQSLKELMH 750
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1357-1829 |
5.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1357 EQLRVKIRKLKNKASVLQKRISEKEEIK--SQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKlriTEEQYR 1434
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL---QEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1435 IEADVTKPIKPALKSAevelktggnnsnqvseTDEKEDLLHENRLMQDEIARLRLEKDTIKNQnleKKYLKDFEIVKRKH 1514
Cdd:COG4717 182 LLEQLSLATEEELQDL----------------AEELEELQQRLAELEEELEEAQEELEELEEE---LEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1515 EDLQKA------------LKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRlnaarcdhd 1582
Cdd:COG4717 243 ERLKEArlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL--------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1583 qshssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLktelhytgEALKEKALVfEHVQSELKQ--KQS 1660
Cdd:COG4717 314 -----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--------EELEEELQL-EELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1661 QMKDIEKMYksgyntmeKCIEKQERFCQLKKQNMLLQQQLDDARNkaDNQEKAILNIQARCDARVQNLQAEcrkhrllLE 1740
Cdd:COG4717 380 GVEDEEELR--------AALEQAEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEELEEE-------LE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1741 EDNKMLvNELnHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK-------GSATKALLDASSRHCTYLEngmqdsRKKL 1813
Cdd:COG4717 443 ELEEEL-EEL-REELAELEAELEQLEEDGELAELLQELEELKAElrelaeeWAALKLALELLEEAREEYR------EERL 514
|
490
....*....|....*.
gi 1034613727 1814 DQMRSQFQEIQDQLTA 1829
Cdd:COG4717 515 PPVLERASEYFSRLTD 530
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1346-1793 |
6.96e-03 |
|
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: 41.50 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1346 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKElcslrfaiQQEKKKRRNVEEVHQKVREK 1425
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1426 LRiTEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEkdtiKNQNLEKKYLK 1505
Cdd:pfam02463 245 LL-RDEQEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1506 DFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETemqsyhcrlnaarcdhdqsh 1585
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA-------------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1586 ssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDI 1665
Cdd:pfam02463 378 --KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1666 EKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQ-EKAILNIQARCDARVQNLQAECRKHRLLLEEDNK 1744
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034613727 1745 MLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLD 1793
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLI 584
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1364-1843 |
7.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1364 RKLKNKASVLQKRISEKEEIKSQLKHEIL-ELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQyRIEADVtkp 1442
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1443 ikpaLKSAEVELKTggnnsnQVSET-DEKEDLLHENRLMQDEIARLRLEKDTIknqnLEKKYLKDFEI--VKRKHEDLQK 1519
Cdd:PRK02224 256 ----LEAEIEDLRE------TIAETeREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDADAeaVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1520 ---ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQ 1596
Cdd:PRK02224 322 rdeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1597 GTVDKcrhlQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFE---------------HVQS-------- 1653
Cdd:PRK02224 402 DAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegspHVETieedrerv 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1654 -ELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAIlniqARCDARVQNLQAEC 1732
Cdd:PRK02224 478 eELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613727 1733 RKHRLLLE------EDNKMLVNELNhSKEKECQYEKEKAER-----------EVAVRQLQQKRDDVLNKGSATKALLDAS 1795
Cdd:PRK02224 554 EEKREAAAeaeeeaEEAREEVAELN-SKLAELKERIESLERirtllaaiadaEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034613727 1796 SRHCTYLENGMQDSR-KKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQK 1843
Cdd:PRK02224 633 RERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| |
